Native Chemical Ligation and Extended Methods: Mechanisms, Catalysis, Scope, and Limitations

[en] The native chemical ligation reaction (NCL) involves reacting a C-terminal peptide thioester with an N-terminal cysteinyl peptide to produce a native peptide bond between the two fragments. This reaction has considerably extended the size of polypeptides and proteins that can be produced by total synthesis and has also numerous applications in bioconjugation, polymer synthesis, material science, and micro- and nanotechnology research. The aim of the present review is to provide a thorough mechanistic overview of NCL and extended methods. The most relevant properties of peptide thioesters, Cys peptides, and common solvents, reagents, additives, and catalysts used for these ligations are presented. Mechanisms, selectivity and reactivity are, whenever possible, discussed through the insights of computational and physical chemistry studies. The inherent limitations of NCL are discussed with insights from the mechanistic standpoint. This review also presents a palette of O,S-, N,S-, or N,Se-acyl shift systems as thioester or selenoester surrogates and discusses the special molecular features that govern reactivity in each case. Finally, the various thiol-based auxiliaries and thiol or selenol amino acid surrogates that have been developed so far are discussed with a special focus on the mechanism of long-range N,S-acyl migrations and selective dechalcogenation reactions. © 2019 American Chemical Society.

Disciplines :

Chemistry

Author, co-author :

Agouridas, V.; UMR CNRS 8204, Centre d'Immunité et d'Infection de Lille, University of Lille, CNRS, Institut Pasteur de Lille, Lille, F-59000, France

El Mahdi, O.; Faculté Polydisciplinaire de Taza, University Sidi Mohamed Ben Abdellah, BP 1223, Taza Gare, Morocco

Diemer, V.; UMR CNRS 8204, Centre d'Immunité et d'Infection de Lille, University of Lille, CNRS, Institut Pasteur de Lille, Lille, F-59000, France

Cargoët, M.; UMR CNRS 8204, Centre d'Immunité et d'Infection de Lille, University of Lille, CNRS, Institut Pasteur de Lille, Lille, F-59000, France

Monbaliu, Jean-Christophe ; Université de Liège - ULiège > Département de chimie (sciences) > Synthèse organique appliquée

Melnyk, O.; UMR CNRS 8204, Centre d'Immunité et d'Infection de Lille, University of Lille, CNRS, Institut Pasteur de Lille, Lille, F-59000, France

Language :

English

Title :

Native Chemical Ligation and Extended Methods: Mechanisms, Catalysis, Scope, and Limitations

Publication date :

2019

Journal title :

Chemical Reviews

ISSN :

0009-2665

eISSN :

1520-6890

Publisher :

American Chemical Society

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 19 June 2019

Statistics

Number of views

198 (2 by ULiège)

Number of downloads

0 (0 by ULiège)

More statistics

Scopus citations^®

328

Scopus citations^®
without self-citations

310

OpenCitations

273

Bibliography

Goesmann, F.; Rosenbauer, H.; Bredehóft, J. H.; Cabane, M.; Ehrenfreund, P.; Gautier, T.; Giri, C.; Kruger, H.; Le Roy, L.; MacDermott, A. J. Organic Compounds on Comet 67P/Churyumov-Gerasimenko Revealed by COSAC Mass Spectrometry. Science 2015, 349, aab0689.
Curtius, T. Ueber die Einwirkung von Chlorbenzoyl auf Glycocollsiber. J. Prakt. Chem. 1881, 24, 239-240.
Fischer, E.; Fourneau, E. Ueber einige Derivate des Glykocolls. Ber. Dtsch. Chem. Ges. 1901, 34, 2868-2877.
Merrifield, R. B. Solid Phase Peptide Synthesis. I. The Synthesis of a Tetrapeptide. J. Am. Chem. Soc. 1963, 85, 2149-2154.
Merrifield, R. B. Solid Phase Synthesis (Nobel Lecture). Angew. Chem., Int. Ed. 1985, 24, 799-810.
Kent, S. B. H. Chemical Synthesis of Peptides and Proteins. Annu. Rev. Biochem. 1988, 57, 957-989.
Raibaut, L.; El Mahdi, O.; Melnyk, O. Solid Phase Protein Chemical Synthesis. Top. Curr. Chem. 2014, 363, 103-154.
Dawson, P. E.; Muir, T. W.; Clark-Lewis, I.; Kent, S. B. H. Synthesis of Proteins by Native Chemical Ligation. Science 1994, 266, 776-779.
Mitchell, N. J.; Malins, L. R.; Liu, X.; Thompson, R. E.; Chan, B.; Radom, L.; Payne, R. J. Rapid Additive-Free Selenocystine-Selenoester Peptide Ligation. J. Am. Chem. Soc. 2015, 137, 14011-14014.
Bode, J. W.; Fox, R. M.; Baucom, K. D. Chemoselective Amide Ligations by Decarboxylative Condensations of N-Alkylhydroxylamines and Ketoacids. Angew. Chem., Int. Ed. 2006, 45, 1248-1252.
Saxon, E.; Armstrong, J. I.; Bertozzi, C. R. A Traceless Staudinger Ligation for the Chemoselective Synthesis of Amide Bonds. Org. Lett. 2000, 2, 2141-2143.
Nilsson, B. L.; Kiessling, L. L.; Raines, R. T. Staudinger Ligation: A Peptide from a Thioester and Azide. Org. Lett. 2000, 2, 1939-1941.
Liu, C. F.; Tam, J. P. Peptide Segment Ligation Strategy without Use of Protecting Groups. Proc. Natl. Acad. Sci. U. S. A. 1994, 91, 6584-6588.
Zhang, Y.; Xu, C.; Lam, H. Y.; Lee, C. L.; Li, X. Protein Chemical Synthesis by Serine and Threonine Ligation. Proc. Natl. Acad. Sci. U. S. A. 2013, 110, 6657-6662.
Kent, S. B. H. Total Chemical Synthesis of Proteins. Chem. Soc. Rev. 2009, 38, 338-351.
Tam, J. P.; Miao, Z. Stereospecific Pseudoproline Ligation of N-Terminal Serine, Threonine, or Cysteine-Containing Unprotected Peptides. J. Am. Chem. Soc. 1999, 121, 9013-9022.
Tam, J. P.; Rao, C.; Liu, C. F.; Shao, J. Specificity and Formation of Unusual Amino Acids of an Amide Ligation Strategy for Unprotected Peptides. Int. J. Pept. Protein Res. 1995, 45, 209-216.
Agouridas, V.; El Mahdi, O.; Cargoét, M.; Melnyk, O. A Statistical View of Protein Chemical Synthesis Using NCL and Extended Methodologies. Bioorg. Med. Chem. 2017, 25, 4938-4945.
Lynen, F.; Reichert, E. Zur Chemischen Struktur der Aktivierten Essigsaure. Angew. Chem. 1951, 63, 47-48.
Kresge, N.; Simoni, R. D.; Hill, R. L. Biotin-Dependent Enzymes: The Work of Feodor Lynen. J. Biol. Chem. 2009, 284, e6-e7.
Wieland, T.; Scháfer, W. Synthese von Oligopeptiden unter Zellmóglichen Bedingungen. Angew. Chem. 1951, 63, 146-147.
Wieland, T.; Scháfer, W.; Bokelmann, E. Uber Peptidsynthesen V. Uber eine Bequeme Darstellungsweise von Acylthiophenolen und ihre Verwendung zu Amid-und Peptid-Synthesen. Liebigs Ann. 1951, 573, 99-104.
Wieland, T.; Scháfer, W. Uber Peptid-Synthesen. 6. Mitteilung. Die Darstellung eininger Aminoacyl-Thiophenole und ihre Umsetzung mit Aminen und Aminosáuren. Liebigs Ann. 1952, 576, 104-109.
Wieland, T.; Bokelmann, E.; Bauer, L.; Lang, H. U.; Lau, H. Uber Peptidsynthesen. 8. Mitteilung. Liebigs Ann. Chem. 1953, 583, 129-148.
Wieland, T.; Bokelmann, E. Das Verhalten Einiger S-Acyl-Aminomercaptane. Liebigs Ann. 1952, 576, 20-34.
Wieland, T. The History of Peptide Chemistry. In Peptides: Synthesis, Structure, and Applications; Gute, B., Ed.; Academic Press: London, 1995; pp 1-38.
Brenner, M.; Zimmermann, J. P.; Wehrmuller, J.; Quitt, P.; Photaki, I. Eine Neue Umlagerungsreaktion und ein Neues Princip zum Aufbau von Peptidketten. Experientia 1955, 11, 397-399.
Brenner, M.; Zimmermann, J. P. Aminoacyleinlagerung. 4. Mitteilung. Erhaltung der Optischen Aktivitát bei Einlagerungsreaktionen an Salicylsáure-Derivaten: Synthese von Salicoyl-Glycyl-LPhenylalanyl-Glycin-Methylester. Helv. Chim. Acta 1958, 41, 467-470.
Kemp, D. S.; Vellaccio, F., Jr. Rapid Intramolecular Acyl Transfer from Phenol to Carbinolamine-Progress toward a New Class of Peptide Coupling Reagent. J. Org. Chem. 1975, 40, 3003-3004.
Kemp, D. S.; Grattan, J. A.; Reczek, J. Peptide Bond Formation by the Amine Capture Principle. J. Org. Chem. 1975, 40, 3465-3466.
Fotouhi, N.; Bowen, B. R.; Kemp, D. S. Resolution of Proline Acylation Problem for Thiol Capture Strategy by Use of a Chloro-Dibenzofuran Template. Int. J. Pept. Protein Res. 1992, 40, 141-147.
Schnolzer, M.; Kent, S. B. H. Constructing Proteins by Dovetailing Unprotected Synthetic Peptides: Backbone-Engineered HIV Protease. Science 1992, 256, 221-225.
Tam, J. P.; Lu, Y. A.; Liu, C. F.; Shao, J. Peptide Synthesis Using Unprotected Peptides through Orthogonal Coupling Methods. Proc. Natl. Acad. Sci. U. S. A. 1995, 92, 12485-12489.
Tam, J. P.; Yu, Q.; Miao, Z. Orthogonal Ligation Strategies for Peptide and Protein. Biopolymers 1999, 51, 311-332.
Coltart, D. M. Peptide Segment Coupling by Prior Ligation and Proximity-Induced Intramolecular Acyl Transfer. Tetrahedron 2000, 56, 3449-3491.
Tam, J. P.; Xu, J.; Eom, K. D. Methods and Strategies of Peptide Ligation. Biopolymers 2001, 60, 194-205.
Trost, B. M. The Atom Economy-a Search for Synthetic Efficiency. Science 1991, 254, 1471-1477.
Pattabiraman, V. R.; Bode, J. W. Rethinking Amide Bond Synthesis. Nature 2011, 480, 471-479.
Hackenberger, C. P.; Schwarzer, D. Chemoselective Ligation and Modification Strategies for Peptides and Proteins. Angew. Chem., Int. Ed. 2008, 47, 10030-10074.
de Figueiredo, R. M.; Suppo, J.-S.; Campagne, J.-M. Nonclassical Routes for Amide Bond Formation. Chem. Rev. 2016, 116, 12029-12122.
Bondalapati, S.; Jbara, M.; Brik, A. Expanding the Chemical Toolbox for the Synthesis of Large and Uniquely Modified Proteins. Nat. Chem. 2016, 8, 407-418.
Topics in Current Chemistry. Protein Ligation and Total Synthesis; Liu, L., Ed.; Springer International Publishing: New York, 2015; Vols. I, II.
Chemical Ligation. Tools for Biomolecule Synthesis and Modification; D'Andrea, L. D., Romanelli, A., Eds.; John Wiley & Sons: New York, 2017.
Pech, A.; Achenbach, J.; Jahnz, M.; Schulzchen, S.; Jarosch, F.; Bordusa, F.; Klussmann, S. A Thermostable D-Polymerase for Mirror-Image PCR. Nucleic Acids Res. 2017, 45, 3997-4005.
Xu, W.; Jiang, W.; Wang, J.; Yu, L.; Chen, J.; Liu, X.; Liu, L.; Zhu, T. F. Total Chemical Synthesis of a Thermostable Enzyme Capable of Polymerase Chain Reaction. Cell Discov. 2017, 3, 17008.
Tam, J. P.; Lu, Y.-A. Synthesis of Large Cyclic Cystine-Knot Peptide by Orthogonal Coupling Strategy Using Unprotected Peptide Precursor. Tetrahedron Lett. 1997, 38, 5599-5602.
Camarero, J. A.; Muir, T. W. Chemoselective Backbone Cyclization of Unprotected Peptides. Chem. Commun. 1997, 1369-1370.
Shao, Y.; Lu, W.; Kent, S. B. H. A Novel Method to Synthesize Cyclic Peptides. Tetrahedron Lett. 1998, 39, 3911-3914.
Camarero, J. A.; Pavel, J.; Muir, T. W. Chemical Synthesis of a Circular Protein Domain: Evidence for Folding-Assisted Cyclization. Angew. Chem., Int. Ed. 1998, 37, 347-349.
Iwai, H.; Pluckthun, A. Circular Beta-Lactamase: Stability Enhancement by Cyclizing the Backbone. FEBS Lett. 1999, 459, 166-172.
Camarero, J. A.; Muir, T. W. Biosynthesis of a Head-to-Tail Cyclized Protein with Improved Biological Activity. J. Am. Chem. Soc. 1999, 121, 5597-5598.
Camarero, J. A.; Fushman, D.; Sato, S.; Giriat, I.; Cowburn, D.; Raleigh, D. P.; Muir, T. W. Rescuing a Destabilized Protein Fold through Backbone Cyclization. J. Mol. Biol. 2001, 308, 1045-1062.
Craik, D. J. Chemistry. Seamless Proteins Tie up their Loose Ends. Science 2006, 311, 1563-1564.
Clark, R. J.; Craik, D. J. Native Chemical Ligation Applied to the Synthesis and Bioengineering of Circular Peptides and Proteins. Biopolymers 2010, 94, 414-422.
White, C. J.; Yudin, A. K. Contemporary Strategies for Peptide Macrocyclization. Nat. Chem. 2011, 3, 509-524.
Wang, C. K.; Gruber, C. W.; Cemazar, M.; Siatskas, C.; Tagore, P.; Payne, N.; Sun, G.; Wang, S.; Bernard, C. C.; Craik, D. J. Molecular Grafting onto a Stable Framework Yields Novel Cyclic Peptides for the Treatment of Multiple Sclerosis. ACS Chem. Biol. 2014, 9, 156-163.
Li, Y.; Gould, A.; Aboye, T.; Bi, T.; Breindel, L.; Shekhtman, A.; Camarero, J. A. Full Sequence Amino Acid Scanning of Theta-Defensin RTD-1 Yields a Potent Anthrax Lethal Factor Protease Inhibitor. J. Med. Chem. 2017, 60, 1916-1927.
McGinty, R. K.; Kim, J.; Chatterjee, C.; Roeder, R. G.; Muir, T. W. Chemically Ubiquitylated Histone H2B Stimulates hDot1LMediated Intranucleosomal Methylation. Nature 2008, 453, 812-816.
Ajish Kumar, K. S.; Haj-Yahya, M.; Olschewski, D.; Lashuel, H. A.; Brik, A. Highly Efficient and Chemoselective Peptide Ubiquitylation. Angew. Chem., Int. Ed. 2009, 48, 8090-8094.
El Oualid, F.; Merkx, R.; Ekkebus, R.; Hameed, D. S.; Smit, J. J.; de Jong, A.; Hilkmann, H.; Sixma, T. K.; Ovaa, H. Chemical Synthesis of Ubiquitin, Ubiquitin-Based Probes, and Diubiquitin. Angew. Chem., Int. Ed. 2010, 49, 10149-10153.
Kumar, K. S.; Spasser, L.; Erlich, L. A.; Bavikar, S. N.; Brik, A. Total Chemical Synthesis of Di-Ubiquitin Chains. Angew. Chem., Int. Ed. 2010, 49, 9126-9131.
Kumar, K. S.; Bavikar, S. N.; Spasser, L.; Moyal, T.; Ohayon, S.; Brik, A. Total Chemical Synthesis of a 304 Amino Acid K48-Linked Tetraubiquitin Protein. Angew. Chem., Int. Ed. 2011, 50, 6137-6141.
Pan, M.; Gao, S.; Zheng, Y.; Tan, X.; Lan, H.; Tan, X.; Sun, D.; Lu, L.; Wang, T.; Zheng, Q.; et al. Quasi-Racemic X-Ray Structures of K27-Linked Ubiquitin Chains Prepared by Total Chemical Synthesis. J. Am. Chem. Soc. 2016, 138, 7429-7435.
Tang, S.; Liang, L.-J.; Si, Y.-Y.; Gao, S.; Wang, J.-X.; Liang, J.; Mei, Z.; Zheng, J.-S.; Liu, L. Practical Chemical Synthesis of Atypical Ubiquitin Chains by Using an Isopeptide-Linked Ub Isomer. Angew. Chem., Int. Ed. 2017, 56, 13333-13337.
Boll, E.; Drobecq, H.; Ollivier, N.; Raibaut, L.; Desmet, R.; Vicogne, J.; Melnyk, O. A Novel PEG-Based Solid Support Enables the Synthesis of > 50 Amino-Acid Peptide Thioesters and the Total Synthesis of a Functional SUMO-1 Peptide Conjugate. Chem. Sci. 2014, 5, 2017-2022.
Boll, E.; Drobecq, H.; Ollivier, N.; Blanpain, A.; Raibaut, L.; Desmet, R.; Vicogne, J.; Melnyk, O. One-Pot Chemical Synthesis of Small Ubiquitin-Like Modifier (SUMO) Protein-Peptide Conjugates Using Bis(2-Sulfanylethyl)Amido Peptide Latent Thioester Surrogates. Nat. Protoc. 2015, 10, 269-292.
Drobecq, H.; Boll, E.; Senechal, M.; Desmet, R.; Saliou, J. M.; Lacapere, J. J.; Mougel, A.; Vicogne, J.; Melnyk, O. A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide-Protein Conjugates. Bioconjugate Chem. 2016, 27, 1540-1546.
Sakamoto, I.; Tezuka, K.; Fukae, K.; Ishii, K.; Taduru, K.; Maeda, M.; Ouchi, M.; Yoshida, K.; Nambu, Y.; Igarashi, J.; et al. Chemical Synthesis of Homogeneous Human Glycosyl-Interferon-Beta That Exhibits Potent Antitumor Activity in Vivo. J. Am. Chem. Soc. 2012, 134, 5428-5431.
Murakami, M.; Okamoto, R.; Izumi, M.; Kajihara, Y. Chemical Synthesis of an Erythropoietin Glycoform Containing a Complex-Type Disialyloligosaccharide. Angew. Chem., Int. Ed. 2012, 51, 3567-3572.
Unverzagt, C.; Kajihara, Y. Chemical Assembly of NGlycoproteins: A Refined Toolbox to Address a Ubiquitous Posttranslational Modification. Chem. Soc. Rev. 2013, 42, 4408-4420.
Reif, A.; Siebenhaar, S.; Troster, A.; Schmalzlein, M.; Lechner, C.; Velisetty, P.; Gottwald, K.; Pohner, C.; Boos, I.; Schubert, V.; et al. Semisynthesis of Biologically Active Glycoforms of the Human Cytokine Interleukin 6. Angew. Chem., Int. Ed. 2014, 53, 12125-12131.
Chiang, K. P.; Jensen, M. S.; McGinty, R. K.; Muir, T. W. A Semisynthetic Strategy to Generate Phosphorylated and Acetylated Histone H2B. ChemBioChem 2009, 10, 2182-2187.
Jbara, M.; Maity, S. K.; Morgan, M.; Wolberger, C.; Brik, A. Chemical Synthesis of Phosphorylated Histone H2A at Tyr57 Reveals Insight into the Inhibition Mode of the SAGA Deubiquitinating Module. Angew. Chem., Int. Ed. 2016, 55, 4972-4976.
Yu, R. R.; Mahto, S. K.; Justus, K.; Alexander, M. M.; Howard, C. J.; Ottesen, J. J. Hybrid Phase Ligation for Efficient Synthesis of Histone Proteins. Org. Biomol. Chem. 2016, 14, 2603-2607.
Li, J.; Li, Y.; He, Q.; Li, Y.; Li, H.; Liu, L. One-Pot Native Chemical Ligation of Peptide Hydrazides Enables Total Synthesis of Modified Histones. Org. Biomol. Chem. 2014, 12, 5435-5441.
Thompson, R. E.; Liu, X.; Ripoll-Rozada, J.; Alonso-Garcia, N.; Parker, B. L.; Pereira, P. J. B.; Payne, R. J. Tyrosine Sulfation Modulates Activity of Tick-Derived Thrombin Inhibitors. Nat. Chem. 2017, 9, 909-917.
Watson, E. E.; Liu, X.; Thompson, R. E.; Ripoll-Rozada, J.; Wu, M.; Alwis, I.; Gori, A.; Loh, C. T.; Parker, B. L.; Otting, G.; et al. Mosquito-Derived Anophelin Sulfoproteins Are Potent Antithrombotics. ACS Cent. Sci. 2018, 4, 468-476.
Wukovitz, S. W.; Yeates, T. O. Why Protein Crystals Favour Some Space-Groups over Others. Nat. Struct. Mol. Biol. 1995, 2, 1062-1067.
Pentelute, B. L.; Mandal, K.; Gates, Z. P.; Sawaya, M. R.; Yeates, T. O.; Kent, S. B. H. Total Chemical Synthesis and X-Ray Structure of Kaliotoxin by Racemic Protein Crystallography. Chem. Commun. 2009, 46, 8174-8176.
Yeates, T. O.; Kent, S. B. H. Racemic Protein Crystallography. Annu. Rev. Biophys. 2012, 41, 41-61.
Mandal, K.; Uppalapati, M.; Ault-Riche, D.; Kenney, J.; Lowitz, J.; Sidhu, S. S.; Kent, S. B. H. Chemical Synthesis and X-Ray Structure of a Heterochiral {D-Protein Antagonist Plus Vascular Endothelial Growth Factor} Protein Complex by Racemic Crystallography. Proc. Natl. Acad. Sci. U. S. A. 2012, 109, 14779-14784.
Avital-Shmilovici, M.; Mandal, K.; Gates, Z. P.; Phillips, N. B.; Weiss, M. A.; Kent, S. B. H. Fully Convergent Chemical Synthesis of Ester Insulin: Determination of the High Resolution X-Ray Structure by Racemic Protein Crystallography. J. Am. Chem. Soc. 2013, 135, 3173-3185.
Schumacher, T. N.; Mayr, L. M.; Minor, D. L., Jr.; Milhollen, M. A.; Burgess, M. W.; Kim, P. S. Identification of D-Peptide Ligands through Mirror-Image Phage Display. Science 1996, 271, 1854-1857.
Mandal, K.; Kent, S. B. H. Total Chemical Synthesis of Biologically Active Vascular Endothelial Growth Factor. Angew. Chem., Int. Ed. 2011, 50, 8029-8033.
Yan, B.; Ye, L.; Xu, W.; Liu, L. Recent Advances in Racemic Protein Crystallography. Bioorg. Med. Chem. 2017, 25, 4953-4965.
Kent, S. B. H.; Sohma, Y.; Liu, S.; Bang, D.; Pentelute, B.; Mandal, K. Through the Looking Glass-a New World of Proteins Enabled by Chemical Synthesis. J. Pept. Sci. 2012, 18, 428-436.
Zhao, L.; Lu, W. Mirror Image Proteins. Curr. Opin. Chem. Biol. 2014, 22, 56-61.
Weinstock, M. T.; Jacobsen, M. T.; Kay, M. S. Synthesis and Folding of a Mirror-Image Enzyme Reveals Ambidextrous Chaperone Activity. Proc. Natl. Acad. Sci. U. S. A. 2014, 111, 11679-11684.
Gao, S.; Pan, M.; Zheng, Y.; Huang, Y.; Zheng, Q.; Sun, D.; Lu, L.; Tan, X.; Tan, X.; Lan, H.; et al. Monomer/Oligomer Quasi-Racemic Protein Crystallography. J. Am. Chem. Soc. 2016, 138, 14497-14502.
Wang, Z.; Xu, W.; Liu, L.; Zhu, T. F. A Synthetic Molecular System Capable of Mirror-Image Genetic Replication and Transcription. Nat. Chem. 2016, 8, 698-704.
Grogan, M. J.; Kaizuka, Y.; Conrad, R. M.; Groves, J. T.; Bertozzi, C. R. Synthesis of Lipidated Green Fluorescent Protein and Its Incorporation in Supported Lipid Bilayers. J. Am. Chem. Soc. 2005, 127, 14383-14387.
Diezmann, F.; Eberhard, H.; Seitz, O. Native Chemical Ligation in the Synthesis of Internally Modified Oligonucleotide-Peptide Conjugates. Biopolymers 2010, 94, 397-404.
Geiermann, A. S.; Polacek, N.; Micura, R. Native Chemical Ligation of Hydrolysis-Resistant 3?-Peptidyl-tRNA Mimics. J. Am. Chem. Soc. 2011, 133, 19068-19071.
Yeo, D. S.; Srinivasan, R.; Uttamchandani, M.; Chen, G. Y.; Zhu, Q.; Yao, S. Q. Cell-Permeable Small Molecule Probes for Site-Specific Labeling of Proteins. Chem. Commun. 2003, 2870-2871.
Scheibner, K. A.; Zhang, Z.; Cole, P. A. Merging Fluorescence Resonance Energy Transfer and Expressed Protein Ligation to Analyze Protein-Protein Interactions. Anal. Biochem. 2003, 317, 226-232.
Reinhardt, U.; Lotze, J.; Zernia, S.; Morl, K.; Beck-Sickinger, A. G.; Seitz, O. Peptide-Templated Acyl Transfer: A Chemical Method for the Labeling of Membrane Proteins on Live Cells. Angew. Chem., Int. Ed. 2014, 53, 10237-10241.
Chen, N.; Liu, J.; Qiao, Z.; Liu, Y.; Yang, Y.; Jiang, C.; Wang, X.; Wang, C. Chemical Proteomic Profiling of Protein NHomocysteinylation with a Thioester Probe. Chem. Sci. 2018, 9, 2826-2830.
Reulen, S. W. A.; Brusselaars, W. W. T.; Langereis, S.; Mulder, W. J. M.; Breurken, M.; Merkx, M. Protein-Liposome Conjugates Using Cysteine-Lipids and Native Chemical Ligation. Bioconjugate Chem. 2007, 18, 590-596.
Cole, C. M.; Brea, R. J.; Kim, Y. H.; Hardy, M. D.; Yang, J.; Devaraj, N. K. Spontaneous Reconstitution of Functional Transmembrane Proteins During Bioorthogonal Phospholipid Membrane Synthesis. Angew. Chem., Int. Ed. 2015, 54, 12738-12742.
Brea, R. J.; Rudd, A. K.; Devaraj, N. K. Nonenzymatic Biomimetic Remodeling of Phospholipids in Synthetic Liposomes. Proc. Natl. Acad. Sci. U. S. A. 2016, 113, 8589-8594.
Brea, R. J.; Cole, C. M.; Lyda, B. R.; Ye, L.; Prosser, R. S.; Sunahara, R. K.; Devaraj, N. K. In Situ Reconstitution of the Adenosine A2A Receptor in Spontaneously Formed Synthetic Liposomes. J. Am. Chem. Soc. 2017, 139, 3607-3610.
Paramonov, S. E.; Gauba, V.; Hartgerink, J. D. Synthesis of Collagen-Like Peptide Polymers by Native Chemical Ligation. Macromolecules 2005, 38, 7555-7561.
Jung, J. P.; Jones, J. L.; Cronier, S. A.; Collier, J. H. Modulating the Mechanical Properties of Self-Assembled Peptide Hydrogels via Native Chemical Ligation. Biomaterials 2008, 29, 2143-2151.
Hu, B.-H.; Su, J.; Messersmith, P. B. Hydrogels Cross-Linked by Native Chemical Ligation. Biomacromolecules 2009, 10, 2194-2200.
Dirksen, A.; Meijer, E. W.; Adriaens, W.; Hackeng, T. M. Strategy for the Synthesis of Multivalent Peptide-Based Nonsymmetric Dendrimers by Native Chemical Ligation. Chem. Commun. 2006, 1667-1669.
Najafi, M.; Kordalivand, N.; Moradi, M.-A.; van den Dikkenberg, J.; Fokkink, R.; Friedrich, H.; Sommerdijk, N. A. J. M.; Hembury, M.; Vermonden, T. Native Chemical Ligation for Cross-Linking of Flower-Like Micelles. Biomacromolecules 2018, 19, 3766-3775.
Byun, E.; Kim, J.; Kang, S. M.; Lee, H.; Bang, D.; Lee, H. Surface PEGylation via Native Chemical Ligation. Bioconjugate Chem. 2011, 22, 4-8.
Helms, B.; van Baal, I.; Merkx, M.; Meijer, E. W. Site-Specific Protein and Peptide Immobilization on a iosensor Surface by Pulsed Native Chemical Ligation. ChemBioChem 2007, 8, 1790-1794.
Wieczerzak, E.; Hamel, R.; Chabot, V.; Aimez, V.; Grandbois, M.; Charette, P. G.; Escher, E. Monitoring of Native Chemical Ligation on Solid Substrate by Surface Plasmon Resonance. Biopolymers 2008, 90, 415-420.
Dendane, N.; Melnyk, O.; Xu, T.; Grandidier, B.; Boukherroub, R.; Stievenard, D.; Coffinier, Y. Direct Characterization of Native Chemical Ligation of Peptides on Silicon Nanowires. Langmuir 2012, 28, 13336-13344.
Schmitt, S. K.; Trebatoski, D. J.; Krutty, J. D.; Xie, A. W.; Rollins, B.; Murphy, W. L.; Gopalan, P. Peptide Conjugation to a Polymer Coating via Native Chemical Ligation of Azlactones for Cell Culture. Biomacromolecules 2016, 17, 1040-1047.
Carpino, L. A.; Han, G. Y. 9-Fluorenylmethoxycarbonyl Function, a New Base-Sensitive Amino-Protecting Group. J. Am. Chem. Soc. 1970, 92, 5748-5749.
Carpino, L. A.; Han, G. Y. 9-Fluorenylmethoxycarbonyl Amino-Protecting Group. J. Org. Chem. 1972, 37, 3404-3409.
Atherton, E.; Fox, H.; Harkiss, D.; Logan, C. J.; Sheppard, R. C.; Williams, B. J. A Mild Procedure for Solid Phase Peptide Synthesis: Use of Fluorenylmethoxycarbonylamino-Acids. J. Chem. Soc., Chem. Commun. 1978, 13, 537-539.
King, D. S.; Fields, C. G.; Fields, G. B. A Cleavage Method which Minimizes Side Reactions Following Fmoc Solid Phase Peptide Synthesis. Int. J. Pept. Protein Res. 1990, 36, 255-266.
Fields, G. B.; Noble, R. L. Solid Phase Peptide Synthesis Utilizing 9-Fluorenylmethoxycarbonyl Amino Acids. Int. J. Pept. Protein Res. 1990, 35, 161-214.
Lenard, J.; Robinson, A. B. Use of Hydrogen Fluoride in Merrifield Solid-Phase Peptide Synthesis. J. Am. Chem. Soc. 1967, 89, 181-182.
Tam, J. P.; Heath, W. F.; Merrifield, R. B. Improved Deprotection in Solid Phase Peptide Synthesis: Removal of Protecting Groups from Synthetic Peptides by an SN2 Mechanism with Low Concentrations of HF in Dimethylsulfide. Tetrahedron Lett. 1982, 23, 4435-4438.
Tam, J. P.; Heath, W. F.; Merrifield, R. B. Improved Deprotection in Solid Phase Peptide Synthesis: Quantitative Reduction of Methionine Sulfoxide to Methionine During HF Cleavage. Tetrahedron Lett. 1982, 23, 2939-2942.
Tam, J. P.; Heath, W. F.; Merrifield, R. B. An SN2 Deprotection of Synthetic Peptides with a Low Concentration of Hydrofluoric Acid in Dimethyl Sulfide: Evidence and Application in Peptide Synthesis. J. Am. Chem. Soc. 1983, 105, 6442-6455.
Raibaut, L.; Ollivier, N.; Melnyk, O. Sequential Native Peptide Ligation Strategies for Total Chemical Protein Synthesis. Chem. Soc. Rev. 2012, 41, 7001-7015.
Offer, J.; Boddy, C. N.; Dawson, P. E. Extending Synthetic Access to Proteins with a Removable Acyl Transfer Auxiliary. J. Am. Chem. Soc. 2002, 124, 4642-4646.
Brik, A.; Ficht, S.; Yang, Y.-Y.; Wong, C.-H. Sugar-Assisted Ligation of N-Linked Glycopeptides with Broad Sequence Tolerance at the Ligation Junction. J. Am. Chem. Soc. 2006, 128, 15026-15033.
Yan, L. Z.; Dawson, P. E. Synthesis of Peptides and Proteins without Cysteine Residues by Native Chemical Ligation Combined with Desulfurization. J. Am. Chem. Soc. 2001, 123, 526-533.
Wan, Q.; Danishefsky, S. J. Free-Radical-Based, Specific Desulfurization of Cysteine: A Powerful Advance in the Synthesis of Polypeptides and Glycopolypeptides. Angew. Chem., Int. Ed. 2007, 46, 9248-9252.
Mills, K. V.; Johnson, M. A.; Perler, F. B. Protein Splicing: How Inteins Escape from Precursor Proteins. J. Biol. Chem. 2014, 289, 14498-14505.
Cappadocia, L.; Lima, C. D. Ubiquitin-Like Protein Conjugation: Structures, Chemistry, and Mechanism. Chem. Rev. 2018, 118, 889-918.
Otto, H.-H.; Schirmeister, T. Cysteine Proteases and their Inhibitors. Chem. Rev. 1997, 97, 133-172.
Jencks, W. P.; Cordes, S.; Carriuolo, J. The Free Energy of Thiol Ester Hydrolysis. J. Biol. Chem. 1960, 235, 3608-3614.
Connors, K. A.; Bender, M. L. The Kinetics of Alkaline Hydrolysis and n-Butylaminolysis of Ethyl p-Nitrobenzoate and Ethyl p-Nitrothiolbenzoate. J. Org. Chem. 1961, 26, 2498-2504.
Barnett, R. E.; Jencks, W. P. Diffusion-Controlled Proton Transfer in Intramolecular Thiol Ester Aminolysis and Thiazoline Hydrolysis. J. Am. Chem. Soc. 1969, 91, 2358-2369.
Hupe, D. J.; Jencks, W. P. Nonlinear Structure-Reactivity Correlations. Acyl Transfer between Sulfur and Oxygen Nucleophiles. J. Am. Chem. Soc. 1977, 99, 451-464.
Bracher, P. J.; Snyder, P. W.; Bohall, B. R.; Whitesides, G. M. The Relative Rates of Thiol-Thioester Exchange and Hydrolysis for Alkyl and Aryl Thioalkanoates in Water. Origins Life Evol. Biospheres 2011, 41, 399-412.
Yang, W.; Drueckhammer, D. G. Computational Studies of the Aminolysis of Oxoesters and Thioesters in Aqueous Solution. Org. Lett. 2000, 2, 4133-4136.
Yang, W.; Drueckhammer, D. G. Understanding the Relative Acyl-Transfer Reactivity of Oxoesters and Thioesters: Computational Analysis of Transition State Delocalization Effects. J. Am. Chem. Soc. 2001, 123, 11004-11009.
Matzke, P.; Chacon, O.; Andrade, C. Normal Coordinate Analysis of Some Esters; Methyl Formate, Methyl Acetate and Dimethyl Oxalate. J. Mol. Struct. 1971, 9, 255-264.
Susi, S.; Scheker, J. R. The Normal Vibrations of Formic Acid and Methyl Formate. Spectrochim. Acta 1969, 25, 1243-1263.
Rey-Lafon, M.; Forel, M. T.; Garrigou-Lagrange, C. Discussion des Modes Normaux des Groupements Amides is et Trans á Partir des Champs de Force du ?-Valérolactame et du NMethylacetamide. Spectrochim. Acta 1973, 29A, 471-486.
El-Assar, A. M. M.; Nash, C. P.; Ingraham, L. L. Infrared and Raman Spectra of S-Methyl Thioacetate: Toward an Understanding of the Biochemical Reactivity of Esters of Coenzyme A. Biochemistry 1982, 21, 1972-1976.
Della Védova, C. O.; Romano, R. M.; Oberhammer, H. Gas Electron Diffraction Analysis on S-Methyl Thioacetate, CH3C(O)-SCH3. J. Org. Chem. 2004, 69, 5395-5398.
Kitano, M.; Fukuyama, T.; Kuchitsu, K. Molecular Structure of N-Methylacetamide as Studied by Gas Electron Diffraction. Bull. Chem. Soc. Jpn. 1973, 46, 384-387.
Pauling, L.; Corey, R. B.; Branson, H. R. The Structure of Proteins; Two Hydrogen-Bonded Helical Configurations of the Polypeptide Chain. Proc. Natl. Acad. Sci. U. S. A. 1951, 37, 205-211.
Henao Castaneda, I. C.; Della Védova, C. O.; Piro, O. E.; Metzler-Nolte, N.; Jios, J. L. Synthesis of Two New Thioesters Bearing Ferrocene: Vibrational Characterization and Ab Initio Calculations. X-Ray Crystal Structure of S-(2-Methoxyphenyl)-Ferrocenecarbothioate. Polyhedron 2010, 29, 827-832.
Erben, M. F.; Boese, R.; Della Védova, C. O.; Oberhammer, H.; Willner, H. Toward an Intimate Understanding of the Structural Properties and Conformational Preference of Oxoesters and Thioesters: Gas and Crystal Structure and Conformational Analysis of Dimethyl Monothiocarbonate, CH3OC(O)SCH3. J. Org. Chem. 2006, 71, 616-622.
Law, S. K.; Dodds, A. W. The Internal Thioester and the Covalent Binding Properties of the Complement Proteins C3 and C4. Protein Sci. 1997, 6, 263-274.
Rangarajan, E. S.; Li, Y.; Ajamian, E.; Iannuzzi, P.; Kernaghan, S. D.; Fraser, M. E.; Cygler, M.; Matte, A. Crystallographic Trapping of the Glutamyl-CoA Thioester Intermediate of Family I CoA Transferases. J. Biol. Chem. 2005, 280, 42919-42928.
Yamaguchi, S.; Kamikubo, H.; Kurihara, K.; Kuroki, R.; Niimura, N.; Shimizu, N.; Yamazaki, Y.; Kataoka, M. Low-Barrier Hydrogen Bond in Photoactive Yellow Protein. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 440-444.
Pointon, J. A.; Smith, W. D.; Saalbach, G.; Crow, A.; Kehoe, M. A.; Banfield, M. J. A Highly Unusual Thioester Bond in a Pilus Adhesin Is Required for Efficient Host Cell Interaction. J. Biol. Chem. 2010, 285, 33858-33866.
Nagy, P. I.; Tejada, F. R.; Sarver, J. G.; Messer, W. S. Conformational Analysis and Derivation of Molecular Mechanics Parameters for Esters and Thioesters. J. Phys. Chem. A 2004, 108, 10173-10185.
Deakyne, C. A.; Ludden, A. K.; Roux, M. V.; Notario, R.; Demchenko, A. V.; Chickos, J. S.; Liebman, J. F. Energetics of the Lighter Chalcogen Analogues of Carboxylic Acid Esters. J. Phys. Chem. B 2010, 114, 16253-16262.
Teixeira-Dias, J. J. C.; Fausto, R.; de Carvalho, L. A. E. B. Conformational Analysis of Carbonyl and Thiocarbonyl Esters: The HC(=X)Y-CH(CH3)2 (X, Y = O or S) Internal Rotation. J. Mol. Struct.: THEOCHEM 1992, 262, 87-103.
Defonsi Lestard, M. E.; Tuttolomondo, M. E.; Ben Altabef, A. Vibrational Spectroscopy and Conformation of S-Ethyl Thioacetate: CH3COSCH2CH3 and Comparison with C(O)S and C(O)O Compounds. Spectrochim. Acta, Part A 2015, 135, 907-914.
Dugarte, N. Y.; Erben, M. F.; Romano, R. M.; Boese, R.; Ge, M. F.; Li, Y.; Della Védova, C. O. Matrix Photochemistry, Photoelectron Spectroscopy, Solid-Phase Structure, and Ring Strain Energy of Beta-Propiothiolactone. J. Phys. Chem. A 2009, 113, 3662-3672.
Dugarte, N. Y.; Erben, M. F.; Romano, R. M.; Ge, M. F.; Li, Y.; Della Védova, C. O. Matrix Photochemistry at Low Temperatures and Spectroscopic Properties of Gamma-Butyrothiolactone. J. Phys. Chem. A 2010, 114, 9462-9470.
Dugarte, N. Y.; Erben, M. F.; Boese, R.; Ge, M. F.; Yao, L.; Della Védova, C. O. Molecular and Electronic Structure of Delta-Valerothiolactone. J. Phys. Chem. A 2010, 114, 12540-12547.
MDowell, P.; Affas, Z.; Reynolds, C.; Holden, M. T.; Wood, S. J.; Saint, S.; Cockayne, A.; Hill, P. J.; Dodd, C. E.; Bycroft, B. W.; et al. Structure, Activity and Evolution of the Group I Thiolactone Peptide Quorum-Sensing System of Staphylococcus aureus. Mol. Microbiol. 2001, 41, 503-512.
Avan, I.; Hall, C. D.; Katritzky, A. R. Peptidomimetics via Modifications of Amino Acids and Peptide Bonds. Chem. Soc. Rev. 2014, 43, 3575-3594.
Kirchdoerfer, R. N.; Garner, A. L.; Flack, C. E.; Mee, J. M.; Horswill, A. R.; Janda, K. D.; Kaufmann, G. F.; Wilson, I. A. Structural Basis for Ligand Recognition and Discrimination of a Quorum-Quenching Antibody. J. Biol. Chem. 2011, 286, 17351-17358.
Negri, A.; Marco, E.; Garcia-Hernandez, V.; Domingo, A.; Llamas-Saiz, A. L.; Porto-Sanda, S.; Riguera, R.; Laine, W.; David-Cordonnier, M. H.; Bailly, C.; et al. Antitumor Activity, X-Ray Crystal Structure, and DNA Binding Properties of Thiocoraline A, a Natural Bisintercalating Thiodepsipeptide. J. Med. Chem. 2007, 50, 3322-3333.
Dugarte, N. Y.; Erben, M. F.; Hey-Hawkins, E.; Lónnecke, P.; Stadlbauer, S.; Ge, M.-F.; Li, Y.; Piro, O. E.; Echeverria, G. A.; Della Védova, C. O. Conformational Transferability of the Sulfenyl Carbonyl Group-SC(O)-in Cyclic Thioesters. J. Phys. Chem. A 2013, 117, 5706-5714.
Um, I.-H.; Kim, G.-R.; Kwon, D.-S. The Effects of Solvation and Polarizability on the Reaction of S-p-Nitrophenyl Thiobenzoate with Various Anionic Nucleophiles. Bull. Korean Chem. Soc. 1994, 15, 585-589.
Flavell, R. R.; Muir, T. W. Expressed Protein Ligation (EPL) in the Study of Signal Transduction, Ion Conduction, and Chromatin Biology. Acc. Chem. Res. 2009, 42, 107-116.
Kang, J.; Macmillan, D. Peptide and Protein Thioester Synthesis via N->S Acyl Transfer. Org. Biomol. Chem. 2010, 8, 1993-2002.
Mende, F.; Seitz, O. 9-Fluorenylmethoxycarbonyl-Based Solid-Phase Synthesis of Peptide ?-Thioesters. Angew. Chem., Int. Ed. 2011, 50, 1232-1240.
Zheng, J.-S.; Tang, S.; Huang, Y.-C.; Liu, L. Development of New Thioester Equivalents for Protein Chemical Synthesis. Acc. Chem. Res. 2013, 46, 2475-2484.
Shah, N. H.; Muir, T. W. Inteins: Nature's Gift to Protein Chemists. Chem. Sci. 2014, 5, 446-461.
Li, H.; Dong, S. Recent Advances in the Preparation of Fmoc-SPPS-Based Peptide Thioester and Its Surrogates for NCL-Type Reactions. Sci. China: Chem. 2017, 60, 201-213.
Muir, T. W.; Sondhi, D.; Cole, P. A. Expressed Protein Ligation: A General Method for Protein Engineering. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 6705-6710.
Evans, T. C., Jr.; Benner, J.; Xu, M. Q. Semisynthesis of Cytotoxic Proteins Using a Modified Protein Splicing Element. Protein Sci. 1998, 7, 2256-2264.
Pellois, J. P.; Muir, T. W. Semisynthetic Proteins in Mechanistic Studies: Using Chemistry to Go Where Nature Can't. Curr. Opin. Chem. Biol. 2006, 10, 487-491.
McGinty, R. K.; Chatterjee, C.; Muir, T. W. Semisynthesis of Ubiquitylated Proteins. Methods Enzymol. 2009, 462, 225-243.
Fierz, B.; Chatterjee, C.; McGinty, R. K.; Bar-Dagan, M.; Raleigh, D. P.; Muir, T. W. Histone H2B Ubiquitylation Disrupts Local and Higher-Order Chromatin Compaction. Nat. Chem. Biol. 2011, 7, 113-119.
Conibear, A. C.; Watson, E. E.; Payne, R. J.; Becker, C. F. W. Native Chemical Ligation in Protein Synthesis and Semi-Synthesis. Chem. Soc. Rev. 2018, 47, 9046-9068.
Shin, Y.; Winans, K. A.; Backes, B. J.; Kent, S. B. H.; Ellman, J. A.; Bertozzi, C. R. Fmoc-Based Synthesis of peptide-?Thioesters: Application to the Total Chemical Synthesis of a Glycoprotein by Native Chemical Ligation. J. Am. Chem. Soc. 1999, 121, 11684-11689.
Alsina, J.; Yokum, T. S.; Albericio, F.; Barany, G. Backbone Amide Linker (Bal) Strategy for N?-9-Fluorenylmethoxycarbonyl (Fmoc) Solid-Phase Synthesis of Unprotected Peptide p-Nitroanilides and Thioesters. J. Org. Chem. 1999, 64, 8761-8769.
Alsina, J.; Kates, S. A.; Barany, G.; Albericio, F. Backbone Amide Linker Strategies for the Solid-Phase Synthesis of C-Terminal Modified Peptides. Methods Mol. Biol. 2005, 298, 195-208.
Ficht, S.; Payne, R. J.; Guy, R. T.; Wong, C.-H. Solid-Phase Synthesis of Peptide and Glycopeptide Thioesters through Side-Chain-Anchoring Strategies. Chem.-Eur. J. 2008, 14, 3620-3629.
Kitagawa, K.; Adachi, H.; Sekigawa, Y.; Yagami, T.; Futaki, S.; Gu, Y. J.; Inoue, K. Total Chemical Synthesis of Large CCK Isoforms Using a Thioester Segment Condensation Approach. Tetrahedron 2004, 60, 907-918.
von Eggelkraut-Gottanka, R.; Klose, A.; Beck-Sickinger, A. G.; Beyermann, M. Peptide ?Thioester Formation Using Standard Fmoc-Chemistry. Tetrahedron Lett. 2003, 44, 3551-3554.
Ingenito, R.; Bianchi, E.; Fattori, D.; Pessi, A. Solid Phase Synthesis of Peptide C-Terminal Thioesters by Fmoc/t-Bu Chemistry. J. Am. Chem. Soc. 1999, 121, 11369-11374.
Kenner, G. W.; McDermott, J. R.; Sheppard, R. C. The Safety Catch Principle in Solid Phase Peptide Synthesis. J. Chem. Soc. D 1971, 636-637.
Backes, B. J.; Virgilio, A. A.; Ellman, J. A. Activation Method to Prepare a Highly Reactive Acylsulfonamide ?Safety-Catch? Linker for Solid-Phase Synthesis. J. Am. Chem. Soc. 1996, 118, 3055-3056.
Backes, B. J.; Ellman, J. A. An Alkanesulfonamide ?Safety-Catch? Linker for Solid-Phase Synthesis. J. Org. Chem. 1999, 64, 2322-2330.
Heidler, P.; Link, A. N-Acyl-N-Alkyl-Sulfonamide Anchors Derived from Kenner's Safety-Catch Linker: Powerful Tools in Bioorganic and Medicinal Chemistry. Bioorg. Med. Chem. 2005, 13, 585-599.
Wieland, T.; Hennig, H. J. Aminosáure-Sulfimide. Chem. Ber. 1960, 93, 1236-1246.
Mezzato, S.; Schaffrath, M.; Unverzagt, C. An Orthogonal Double-Linker Resin Facilitates the Efficient Solid-Phase Synthesis of Complex-Type N-Glycopeptide Thioesters Suitable for Native Chemical Ligation. Angew. Chem., Int. Ed. 2005, 44, 1650-1654.
Quaderer, R.; Hilvert, D. Improved Synthesis of C-Terminal Peptide Thioesters on ?Safety-Catch? Resins Using LiBr/THF. Org. Lett. 2001, 3, 3181-3184.
Burlina, F.; Morris, C.; Behrendt, R.; White, P.; Offer, J. Simplifying Native Chemical Ligation with an N-Acylsulfonamide Linker. Chem. Commun. 2012, 48, 2579-2581.
Ollivier, N.; Behr, J. B.; El-Mahdi, O.; Blanpain, A.; Melnyk, O. Fmoc Solid-Phase Synthesis of Peptide Thioesters Using an Intramolecular N, S-Acyl Shift. Org. Lett. 2005, 7, 2647-2650.
Mende, F.; Seitz, O. Solid-Phase Synthesis of Peptide Thioesters with Self-Purification. Angew. Chem., Int. Ed. 2007, 46, 4577-4580.
Mende, F.; Beisswenger, M.; Seitz, O. Automated Fmoc-Based Solid-Phase Synthesis of Peptide Thioesters with Self-Purification Effect and Application in the Construction of Immobilized SH3 Domains. J. Am. Chem. Soc. 2010, 132, 11110-11118.
Blanco-Canosa, J. B.; Dawson, P. E. An Efficient Fmoc-SPPS Approach for the Generation of Thioester Peptide Precursors for Use in Native Chemical Ligation. Angew. Chem., Int. Ed. 2008, 47, 6851-6855.
Tofteng, A. P.; Sørensen, K. K.; Conde-Frieboes, K. W.; Hoeg-Jensen, T.; Jensen, K. J. Fmoc Solid-Phase Synthesis of C-Terminal Peptide Thioesters by Formation of a Backbone Pyroglutamyl Imide Moiety. Angew. Chem., Int. Ed. 2009, 48, 7411-7414.
Mahto, S. K.; Howard, C. J.; Shimko, J. C.; Ottesen, J. J. A Reversible Protection Strategy to Improve Fmoc-SPPS of Peptide Thioesters by the N-Acylurea Approach. ChemBioChem 2011, 12, 2488-2494.
Blanco-Canosa, J. B.; Nardone, B.; Albericio, F.; Dawson, P. E. Chemical Protein Synthesis Using a Second-Generation N-Acylurea Linker for the Preparation of Peptide-Thioester Precursors. J. Am. Chem. Soc. 2015, 137, 7197-7209.
Elashal, H. E.; Sim, Y. E.; Raj, M. Serine Promoted Synthesis of Peptide Thioester-Precursor on Solid Support for Native Chemical Ligation. Chem. Sci. 2017, 8, 117-123.
Pascal, R.; Chauvey, D.; Sola, R. Carboxyl-Protecting Groups Convertible into Activating Groups. Carbamates of o-Aminoanilides Are Precursors of Reactive N-Acylureas. Tetrahedron Lett. 1994, 35, 6291-6294.
Pala-Pujadas, J.; Albericio, F.; Blanco-Canosa, J. B. Peptide Ligations by Using Aryloxycarbonyl-o-Methylaminoanilides: Chemical Synthesis of Palmitoylated Sonic Hedgehog. Angew. Chem., Int. Ed. 2018, 57, 16120-16125.
Weidmann, J.; Dimitrijevic?, E.; Hoheisel, J. D.; Dawson, P. E. Boc-SPPS: Compatible Linker for the Synthesis of Peptide o-Aminoanilides. Org. Lett. 2016, 18, 164-167.
Sola, R.; Saguer, P.; David, M.-L.; Pascal, R. A New Type of Safety-Catch Linker Cleaved by Intramolecular Activation of an Amide Anchorage and Allowing Aqueous Processing in Solid-Phase Peptide Synthesis. J. Chem. Soc., Chem. Commun. 1993, 1786-1788.
Fang, G.-M.; Li, Y.-M.; Shen, F.; Huang, Y.-C.; Li, J.-B.; Lin, Y.; Cui, H.-K.; Liu, L. Protein Chemical Synthesis by Ligation of Peptide Hydrazides. Angew. Chem., Int. Ed. 2011, 50, 7645-7649.
Millington, C. R.; Quarrell, R.; Lowe, G. Aryl Hydrazides as Linkers for Solid Phase Synthesis which Are Cleavable under Mild Oxidative Conditions. Tetrahedron Lett. 1998, 39, 7201-7204.
Camarero, J. A.; Hackel, B. J.; de Yoreo, J. J.; Mitchell, A. R. Fmoc-Based Synthesis of Peptide ?-thioesters Using an Aryl Hydrazine Support. J. Org. Chem. 2004, 69, 4145-4151.
Ingenito, R.; Wenschuh, H. Effect of Copper Salts on Peptide Bond Formation Using Peptide Thioesters. Org. Lett. 2003, 5, 4587-4590.
Zheng, J. S.; Tang, S.; Guo, Y.; Chang, H. N.; Liu, L. Synthesis of Cyclic Peptides and Cyclic Proteins via Ligation of Peptide Hydrazides. ChemBioChem 2012, 13, 542-546.
Zheng, J.-S.; Tang, S.; Qi, Y.-K.; Wang, Z.-P.; Liu, L. Chemical Synthesis of Proteins Using Peptide Hydrazides as Thioester Surrogates. Nat. Protoc. 2013, 8, 2483-2495.
Meienhofer, J. The Azide Method in Peptide Synthesis. In The Peptides. Analysis, Synthesis, Biology; Gross, E., Meienhofer, J., Eds.; Academic Press: New York, 1979, Vol 1, pp 197-239.
Vinogradov, A. A.; Simon, M. D.; Pentelute, B. L. C-Terminal Modification of Fully Unprotected Peptide Hydrazides via in Situ Generation of Isocyanates. Org. Lett. 2016, 18, 1222-1225.
Huang, Y.-C.; Chen, C.-C.; Li, S.-J.; Gao, S.; Shi, J.; Li, Y.-M. Facile Synthesis of C-Terminal Peptide Hydrazide and Thioester of NY-ESO-1 (A39-A68) from an Fmoc-Hydrazine 2-Chlorotrityl Chloride Resin. Tetrahedron 2014, 70, 2951-2955.
Thompson, R. E.; Liu, X.; Alonso-Garcia, N.; Pereira, P. J.; Jolliffe, K. A.; Payne, R. J. Trifluoroethanethiol: An Additive for Efficient One-Pot Peptide Ligation-Desulfurization Chemistry. J. Am. Chem. Soc. 2014, 136, 8161-8164.
Tian, X.; Li, J.; Huang, W. Optimal Peptide Hydrazide Ligation with C-Terminus Asp, Asn, and Gln Hydrazides. Tetrahedron Lett. 2016, 57, 4264-4267.
Siman, P.; Karthikeyan, S. V.; Nikolov, M.; Fischle, W.; Brik, A. Convergent Chemical Synthesis of Histone H2B Protein for the Site-Specific Ubiquitination at Lys34. Angew. Chem., Int. Ed. 2013, 52, 8059-8063.
Thom, J.; Anderson, D.; McGregor, J.; Cotton, G. Recombinant Protein Hydrazides: Application to Site-Specific Protein PEGylation. Bioconjugate Chem. 2011, 22, 1017-1020.
Li, Y. M.; Yang, M. Y.; Huang, Y. C.; Li, Y. T.; Chen, P. R.; Liu, L. Ligation of Expressed Protein Alpha-Hydrazides via Genetic Incorporation of an Alpha-Hydroxy Acid. ACS Chem. Biol. 2012, 7, 1015-1022.
Li, Y.-M.; Li, Y.-T.; Pan, M.; Kong, X.-Q.; Huang, Y.-C.; Hong, Z.-Y.; Liu, L. Irreversible Site-Specific Hydrazinolysis of Proteins by Use of Sortase. Angew. Chem., Int. Ed. 2014, 53, 2198-2202.
Adams, A. L.; Cowper, B.; Morgan, R. E.; Premdjee, B.; Caddick, S.; Macmillan, D. Cysteine Promoted C-Terminal Hydrazinolysis of Native Peptides and Proteins. Angew. Chem., Int. Ed. 2013, 52, 13062-13066.
Wang, J. X.; Fang, G. M.; He, Y.; Qu, D. L.; Yu, M.; Hong, Z. Y.; Liu, L. Peptide o-Aminoanilides as Crypto-Thioesters for Protein Chemical Synthesis. Angew. Chem., Int. Ed. 2015, 54, 2194-2198.
Katritzky, A. R.; Shestopalov, A. A.; Suzuki, K. A New Convenient Preparation of Thiol Esters Utilizing N-Acylbenzotriazoles. Synthesis 2004, 2004, 1806-1813.
Selvaraj, A.; Chen, H.-T.; Ya-Ting Huang, A.; Kao, C.-L. Expedient on-Resin Modification of a Peptide C-Terminus through a Benzotriazole Linker. Chem. Sci. 2018, 9, 345-349.
Flood, D. T.; Hintzen, J. C. J.; Bird, M. J.; Cistrone, P. A.; Chen, J. S.; Dawson, P. E. Leveraging the Knorr Pyrazole Synthesis for the Facile Generation of Thioester Surrogates for Use in Native Chemical Ligation. Angew. Chem., Int. Ed. 2018, 57, 11634-11639.
Pira, S. L.; El Mahdi, O.; Raibaut, L.; Drobecq, H.; Dheur, J.; Boll, E.; Melnyk, O. Insight into the SEA Amide Thioester Equilibrium. Application to the Synthesis of Thioesters at Neutral pH. Org. Biomol. Chem. 2016, 14, 7211-7216.
Nagaike, F.; Onuma, Y.; Kanazawa, C.; Hojo, H.; Ueki, A.; Nakahara, Y.; Nakahara, Y. Efficient Microwave-Assisted Tandem Nto S-Acyl Transfer and Thioester Exchange for the Preparation of a Glycosylated Peptide Thioester. Org. Lett. 2006, 8, 4465-4468.
Hojo, H.; Onuma, Y.; Akimoto, Y.; Nakahara, Y.; Nakahara, Y. N-Alkyl Cysteine-Assisted Thioesterification of Peptides. Tetrahedron Lett. 2007, 48, 25-28.
Nakamura, K.; Mori, H.; Kawakami, T.; Hojo, H.; Nakahara, Y.; Aimoto, S. Peptide Thioester Synthesis via an Auxiliary-Mediated N-S Acyl Shift Reaction in Solution. Int. J. Pept. Res. Ther. 2007, 13, 191-202.
Kang, J.; Richardson, J. P.; Macmillan, D. 3-Mercaptopropionic Acid-Mediated Synthesis of Peptide and Protein Thioesters. Chem. Commun. 2009, 407-409.
Tsuda, S.; Shigenaga, A.; Bando, K.; Otaka, A. N. S. Acyl-Transfer-Mediated Synthesis of Peptide Thioesters Using Anilide Derivatives. Org. Lett. 2009, 11, 823-826.
Erlich, L. A.; Kumar, K. S.; Haj-Yahya, M.; Dawson, P. E.; Brik, A. N-Methylcysteine-Mediated Total Chemical Synthesis of Ubiquitin Thioester. Org. Biomol. Chem. 2010, 8, 2392-2396.
Dheur, J.; Ollivier, N.; Vallin, A.; Melnyk, O. Synthesis of Peptide Alkylthioesters Using the Intramolecular N, S-Acyl Shift Properties of Bis(2-Sulfanylethyl)Amido Peptides. J. Org. Chem. 2011, 76, 3194-3202.
Sharma, R. K.; Tam, J. P. Tandem Thiol Switch Synthesis of Peptide Thioesters via N-S Acyl Shift on Thiazolidine. Org. Lett. 2011, 13, 5176-5179.
Taichi, M.; Hemu, X.; Qiu, Y.; Tam, J. P. A Thioethylalkylamido (TEA) Thioester Surrogate in the Synthesis of a Cyclic Peptide via a Tandem Acyl Shift. Org. Lett. 2013, 15, 2620-2623.
Eto, M.; Naruse, N.; Morimoto, K.; Yamaoka, K.; Sato, K.; Tsuji, K.; Inokuma, T.; Shigenaga, A.; Otaka, A. Development of an Anilide-Type Scaffold for the Thioester Precursor N-Sulfanylethylcoumarinyl Amide. Org. Lett. 2016, 18, 4416-4419.
Shelton, P. M.; Weller, C. E.; Chatterjee, C. A Facile NMercaptoethoxyglycinamide (MEGA) Linker Approach to Peptide Thioesterification and Cyclization. J. Am. Chem. Soc. 2017, 139, 3946-3949.
Cargoét, M.; Diemer, V.; Snella, B.; Desmet, R.; Blanpain, A.; Drobecq, H.; Agouridas, V.; Melnyk, O. Catalysis of Thiol-Thioester Exchange by Water-Soluble Alkyldiselenols Applied to the Synthesis of Peptide Thioesters and SEA-Mediated Ligation. J. Org. Chem. 2018, 83, 12584-12594.
Ollivier, N.; Dheur, J.; Mhidia, R.; Blanpain, A.; Melnyk, O. Bis(2-Sulfanylethyl)Amino Native Peptide Ligation. Org. Lett. 2010, 12, 5238-5241.
Zheng, J. S.; Chang, H. N.; Wang, F. L.; Liu, L. Fmoc Synthesis of Peptide Thioesters without Post-Chain-Assembly Manipulation. J. Am. Chem. Soc. 2011, 133, 11080-11083.
Dheur, J.; Ollivier, N.; Melnyk, O. Synthesis of Thiazolidine Thioester Peptides and Acceleration of Native Chemical Ligation. Org. Lett. 2011, 13, 1560-1563.
Zheng, J.-S.; Xi, W.-X.; Wang, F.-L.; Li, J.; Guo, Q.-X. Fmoc-SPPS Chemistry Compatible Approach for the Generation of (Glyco)Peptide Aryl Thioesters. Tetrahedron Lett. 2011, 52, 2655-2660.
Eom, K. D.; Tam, J. P. Acid-Catalyzed Tandem Thiol Switch for Preparing Peptide Thioesters from Mercaptoethyl Esters. Org. Lett. 2011, 13, 2610-2613.
Liu, F.; Mayer, J. P. An Fmoc Compatible, O to S Shift-Mediated Procedure for the Preparation of C-Terminal Thioester Peptides. J. Org. Chem. 2013, 78, 9848-9856.
Ueda, S.; Fujita, M.; Tamamura, H.; Fujii, N.; Otaka, A. Photolabile Protection for One-Pot Sequential Native Chemical Ligation. ChemBioChem 2005, 6, 1983-1986.
Aihara, K.; Yamaoka, K.; Naruse, N.; Inokuma, T.; Shigenaga, A.; Otaka, A. One-Pot/Sequential Native Chemical Ligation Using Photocaged Crypto-Thioester. Org. Lett. 2016, 18, 596-599.
Kawakami, T.; Aimoto, S. A Photoremovable Ligation Auxiliary for Use in Polypeptide Synthesis. Tetrahedron Lett. 2003, 44, 6059-6061.
Chatterjee, C.; McGinty, R. K.; Pellois, J. P.; Muir, T. W. Auxiliary-Mediated Site-Specific Peptide Ubiquitylation. Angew. Chem., Int. Ed. 2007, 46, 2814-2818.
Pardo, A.; Hogenauer, T. J.; Cai, Z.; Vellucci, J. A.; Castillo, E. M.; Dirk, C. W.; Franz, A. H.; Michael, K. Efficient Photochemical Synthesis of Peptide-?-Phenylthioesters. ChemBioChem 2015, 16, 1884-1889.
Hojo, H.; Aimoto, S. Polypeptide Synthesis Using the S-Alkyl Thioester of a Partially Protected Peptide Segment. Synthesis of the DNA-Binding Domain of c-Myb Protein (142-193)-NH2. Bull. Chem. Soc. Jpn. 1991, 64, 111-117.
Hackeng, T. M.; Griffin, J. H.; Dawson, P. E. Protein Synthesis by Native Chemical Ligation: Expanded Scope by Using Straightforward Methodology. Proc. Natl. Acad. Sci. U. S. A. 1999, 96, 10068-10073.
Brik, A.; Keinan, E.; Dawson, P. E. Protein Synthesis by Solid-Phase Chemical Ligation Using a Safety Catch Linker. J. Org. Chem. 2000, 65, 3829-3835.
Brust, A.; Schroeder, C. I.; Alewood, P. F. High-Throughput Synthesis of Peptide Alpha-Thioesters: A Safety Catch Linker Approach Enabling Parallel Hydrogen Fluoride Cleavage. Chem-MedChem 2014, 9, 1038-1046.
Sato, T.; Saito, Y.; Aimoto, S. Synthesis of the C-Terminal Region of Opioid Receptor Like 1 in an SDS Micelle by the Native Chemical Ligation: Effect of Thiol Additive and SDS Concentration on Ligation Efficiency. J. Pept. Sci. 2005, 11, 410-416.
Johnson, E. C. B.; Kent, S. B. H. Towards the Total Chemical Synthesis of Integral Membrane Proteins: A General Method for the Synthesis of Hydrophobic Peptide-?-Thioester Building Blocks. Tetrahedron Lett. 2007, 48, 1795-1799.
Johnson, E. C. B.; Malito, E.; Shen, Y.; Rich, D.; Tang, W.-J.; Kent, S. B. H. Modular Total Chemical Synthesis of a Human Immunodeficiency Virus Type 1 Protease. J. Am. Chem. Soc. 2007, 129, 11480-11490.
Harris, P. W. R.; Brimble, M. A. Toward the Total Chemical Synthesis of the Cancer Protein NY-ESO-1. Biopolymers 2010, 94, 542-550.
Patek, M.; Lebl, M. A Safety-Catch Type of Amide Protecting Group. Tetrahedron Lett. 1990, 31, 5209-5212.
Nicolas, E.; Vilaseca, M.; Giralt, E. A Study of the Use of NH4I for the Reduction of Methionine Sulfoxide in Peptides Containing Cysteine and Cystine. Tetrahedron 1995, 51, 5701-5710.
Bang, D.; Pentelute, B. L.; Gates, Z. P.; Kent, S. B. H. Direct on-Resin Synthesis of Peptide-Alpha Thiophenylesters for Use in Native Chemical Ligation. Org. Lett. 2006, 8, 1049-1052.
Schnolzer, M.; Alewood, P.; Jones, A.; Alewood, D.; Kent, S. B. H. In Situ Neutralization in Boc-Chemistry Solid Phase Peptide Synthesis. Rapid, High Yield Assembly of Difficult Sequences. Int. J. Pept. Protein Res. 1992, 40, 180-193.
Raz, R.; Burlina, F.; Ismail, M.; Downward, J.; Li, J.; Smerdon, S. J.; Quibell, M.; White, P. D.; Offer, J. HF-Free Boc Synthesis of Peptide Thioesters for Ligation and Cyclization. Angew. Chem., Int. Ed. 2016, 55, 13174-13179.
Li, X.; Kawakami, T.; Aimoto, S. Direct Preparation of Peptide Thioesters Using an Fmoc Solid-Phase Method. Tetrahedron Lett. 1998, 39, 8669-8672.
Hasegawa, K.; Sha, Y. L.; Bang, J. K.; Kawakami, T.; Akaji, K.; Aimoto, S. Preparation of Phosphopeptide Thioesters by Fmoc-and Fmoc(2-F)-Solid Phase Synthesis. Lett. Pept. Sci. 2001, 8, 277-284.
Raz, R.; Rademann, J. Fmoc-Based Synthesis of Peptide Thioesters for Native Chemical Ligation Employing a tert-Butyl Thiol Linker. Org. Lett. 2011, 13, 1606-1609.
Clippingdale, A. B.; Barrow, C. J.; Wade, J. D. Peptide Thioester Preparation by Fmoc Solid Phase Peptide Synthesis for Use in Native Chemical Ligation. J. Pept. Sci. 2000, 6, 225-234.
Bu, X.; Xie, G.; Law, C. W.; Guo, Z. An Improved Deblocking Agent for Direct Fmoc Solid-Phase Synthesis of Peptide Thioesters. Tetrahedron Lett. 2002, 43, 2419-2422.
Brask, J.; Albericio, F.; Jensen, K. J. Fmoc Solid-Phase Synthesis of Peptide Thioesters by Masking as Trithioortho Esters. Org. Lett. 2003, 5, 2951-2953.
Sharma, I.; Crich, D. Direct Fmoc-Chemistry-Based Solid-Phase Synthesis of Peptidyl Thioesters. J. Org. Chem. 2011, 76, 6518-6524.
Hackenberger, C. P. R. The Reduction of Oxidized Methionine Residues in Peptide Thioesters with NH4I-Me2S. Org. Biomol. Chem. 2006, 4, 2291-2295.
Aucagne, V.; Valverde, I. E.; Marceau, P.; Galibert, M.; Dendane, N.; Delmas, A. F. Towards the Simplification of Protein Synthesis: Iterative Solid-Supported Ligations with Concomitant Purifications. Angew. Chem., Int. Ed. 2012, 51, 11320-11324.
Ollivier, N.; Desmet, R.; Drobecq, H.; Blanpain, A.; Boll, E.; Leclercq, B.; Mougel, A.; Vicogne, J.; Melnyk, O. A Simple and Traceless Solid Phase Method Simplifies the Assembly of Large Peptides and the Access to Challenging Proteins. Chem. Sci. 2017, 8, 5362-5370.
Fang, G.-M.; Wang, J.-X.; Liu, L. Convergent Chemical Synthesis of Proteins by Ligation of Peptide Hydrazides. Angew. Chem., Int. Ed. 2012, 51, 10347-10350.
Ollivier, N.; Vicogne, J.; Vallin, A.; Drobecq, H.; Desmet, R.; El-Mahdi, O.; Leclercq, B.; Goormachtigh, G.; Fafeur, V.; Melnyk, O. A One-Pot Three-Segment Ligation Strategy for Protein Chemical Synthesis. Angew. Chem., Int. Ed. 2012, 51, 209-213.
Raibaut, L.; Cargoét, M.; Ollivier, N.; Chang, Y. M.; Drobecq, H.; Boll, E.; Desmet, R.; Monbaliu, J.-C. M.; Melnyk, O. Accelerating Chemoselective Peptide Bond Formation Using Bis(2-Selenylethyl)-Amido Peptide Selenoester Surrogates. Chem. Sci. 2016, 7, 2657-2665.
Raibaut, L.; Adihou, H.; Desmet, R.; Delmas, A. F.; Aucagne, V.; Melnyk, O. Highly Efficient Solid Phase Synthesis of Large Polypeptides by Iterative Ligations of Bis(2-Sulfanylethyl)Amido (SEA) Peptide Segments. Chem. Sci. 2013, 4, 4061-4066.
Okamoto, R.; Morooka, K.; Kajihara, Y. A Synthetic Approach to a Peptide ?-Thioester from an Unprotected Peptide through Cleavage and Activation of a Specific Peptide Bond by NAcetylguanidine. Angew. Chem., Int. Ed. 2012, 51, 191-196.
Orii, R.; Sakamoto, N.; Fukami, D.; Tsuda, S.; Izumi, M.; Kajihara, Y.; Okamoto, R. Total Synthesis of O-Galnacylated Antifreeze Glycoprotein Using the Switchable Reactivity of Peptidyl-N-Pivaloylguanidine. Chem.-Eur. J. 2017, 23, 9253-9257.
Hodson, A. G. W.; Thind, R. K.; McPartlin, M. Synthesis and Reactivity of Organochalogen Ester Substituted ?3-Butadienyl Complexes of Mo(II): Crystal Structure of [MoCl(CO)2(?3-CH2C-(COSePh)C = CH2)(1, 10-Phenanthroline)]0. 5 CH2Cl2. J. Organomet. Chem. 2002, 664, 277-287.
Koketsu, M.; Mizutani, K.; Ogawa, T.; Takahashi, A.; Ishihara, H. Synthesis of 3-Acyl-1-Alkyl-2-Alkylseleno-1-Cyclobutene Using Alkyneselenolate. J. Org. Chem. 2004, 69, 8938-8941.
Mautner, H. G.; Chu, S.-H.; Gunther, W. H. H. The Aminolysis of Thioacyl and Selenoacyl Analogs. J. Am. Chem. Soc. 1963, 85, 3458-3462.
Chu, S.-H.; Mautner, H. G. Analogs of Neuroeffectors. V. Neighboring-Group Effects in the Reactions of Esters, Thiolesters, and Selenolesters. The Hydrolysis and Aminolysis of Benzoylcholine, Benzoylthiolcholine, Benzoylselenolcholine, and of their Dimethylamino Analogs. J. Org. Chem. 1966, 31, 308-312.
Jakubke, H. D. Uber die Verwendung von Aminosáure-und Peptidverbindungen des Selenophenols als "Aktivierte Ester" zur Peptidsynthese. Z. Chem. 1963, 3, 65-66.
Jakubke, H.-D. Synthese von Aminoacyl-und Peptidyl-Selenophenolen und deren Verwendung zur Darstellung Linearer und Cyclischer Peptide. Chem. Ber. 1964, 97, 2816-2828.
Jakubke, H. D. Die Verwendung Aktivierter Ester zur Peptidsynthese. Z. Chem. 1966, 6, 52-67.
Temperini, A.; Terlizzi, R.; Testaferri, L.; Tiecco, M. Stereospecific Synthesis of ?3-Amino Acid Derivatives from Propargylic Alcohols: Efficient Solution-Phase Synthesis of Oligopeptides without Coupling Agents. Chem.-Eur. J. 2009, 15, 7883-7895.
Temperini, A.; Capperucci, A.; Degl'Innocenti, A.; Terlizzi, R.; Tiecco, M. A Reasonably Stereospecific Multistep Conversion of Boc-Protected ?-Amino Acids to Phth-Protected ?3-Amino Acids. Tetrahedron Lett. 2010, 51, 4121-4124.
Sancineto, L.; Pinto Vargas, J.; Monti, B.; Arca, M.; Lippolis, V.; Perin, G.; Lenardao, E.; Santi, C. Atom Efficient Preparation of Zinc Selenates for the Synthesis of Selenol Esters under ?on Water? Conditions. Molecules 2017, 22, 953.
Temperini, A.; Piazzolla, F.; Minuti, L.; Curini, M.; Siciliano, C. General, Mild, and Metal-Free Synthesis of Phenyl Selenoesters from Anhydrides and their Use in Peptide Synthesis. J. Org. Chem. 2017, 82, 4588-4603.
Durek, T.; Alewood, P. F. Preformed Selenoesters Enable Rapid Native Chemical Ligation at Intractable Sites. Angew. Chem., Int. Ed. 2011, 50, 12042-12045.
Singh, U.; Ghosh, S. K.; Chadha, M. S.; Mamdapur, V. R. A New Convenient Approach to Peptide Synthesis Using a Diselenide and a Phosphine. Tetrahedron Lett. 1991, 32, 255-258.
Diver, S. T.; Dermenci, A. Tributylphosphine. In e-EROS; John Wiley & Sons, Ltd, 2001; DOI: 10. 1002/ 047084289X. rt173. pub2.
Hanna, C. C.; Kulkarni, S. S.; Watson, E. E.; Premdjee, B.; Payne, R. J. Solid-Phase Synthesis of Peptide Selenoesters via a Side-Chain Anchoring Strategy. Chem. Commun. 2017, 53, 5424-5427.
Makriyannis, A.; Guenther, W. H. H.; Mautner, H. G. Selenol Esters as Specific Reagents of the Acylation of Thiol Groups. J. Am. Chem. Soc. 1973, 95, 8403-8406.
Takei, T.; Andoh, T.; Takao, T.; Hojo, H. One-Pot Four-Segment Ligation Using Seleno-and Thioesters: Synthesis of Superoxide Dismutase. Angew. Chem., Int. Ed. 2017, 56, 15708-15711.
Ghassemian, A.; Vila-Farres, X.; Alewood, P. F.; Durek, T. Solid Phase Synthesis of Peptide-Selenoesters. Bioorg. Med. Chem. 2013, 21, 3473-3478.
Moroder, L. Isosteric Replacement of Sulfur with Other Chalcogens in Peptides and Proteins. J. Pept. Sci. 2005, 11, 187-214.
Poole, L. B. The Basics of Thiols and Cysteines in Redox Biology and Chemistry. Free Radical Biol. Med. 2015, 80, 148-157.
Thurlkill, R. L.; Grimsley, G. R.; Scholtz, J. M.; Pace, C. N. pK Values of the Ionizable Groups of Proteins. Protein Sci. 2006, 15, 1214-1218.
Bulaj, G.; Kortemme, T.; Goldenberg, D. P. Ionization-Reactivity Relationships for Cysteine Thiols in Polypeptides. Biochemistry 1998, 37, 8965-8972.
Grimsley, G. R.; Scholtz, J. M.; Pace, C. N. A Summary of the Measured pK Values of the Ionizable Groups in Folded Proteins. Protein Sci. 2008, 18, 247-251.
Benesch, R. E.; Benesch, R. The Acid Strength of the-SH Group in Cysteine and Related Compounds. J. Am. Chem. Soc. 1955, 77, 5877-5881.
Nagy, P.; Winterbourn, C. C. Redox Chemistry of Biological Thiols. In Advances in Molecular Toxicology; Fishbein, J. C., Ed.; Elsevier, 2010; Vol. 4, pp 183-222.
Jencks, W. P.; Regenstein, J. Ionization Constants of Acids and Bases. In Handbook of Biochemistry and Molecular Biology; Lundblad, R. L., MacDonald, F. M., Eds.; CRC: New York, 2010; Vol. 67, pp 595-635.
Xan, J.; Wilson, E. A.; Roberts, L. D.; Horton, N. H. The Absorption of Oxygen by Mercaptans in Alkaline Solution. J. Am. Chem. Soc. 1941, 63, 1139-1141.
Wallace, T. J.; Schriesheim, A. Solvent Effects in the Base-Catalyzed Oxidation of Mercaptans with Molecular Oxygen. J. Org. Chem. 1962, 27, 1514-1516.
Wallace, T. J.; Schriesheim, A.; Bartok, W. The Base-Catalyzed Oxidation of Mercaptans. III. Role of the Solvent and Effect of Mercaptan Structure on the Rate Determining Step. J. Org. Chem. 1963, 28, 1311-1314.
Bagiyan, G. A.; Koroleva, I. K.; Soroka, N. V.; Ufimtsev, A. V. Oxidation of Thiol Compounds by Molecular Oxygen in Aqueous Solutions. Russ. Chem. Bull. 2003, 52, 1135-1141.
Dénés, F.; Pichowicz, M.; Povie, G.; Renaud, P. Thiyl Radicals in Organic Synthesis. Chem. Rev. 2014, 114, 2587-2693.
Wallace, T. J.; Schriesheim, A.; Hurwitz, H.; Glaser, M. B. Base-Catalyzed Oxidation of Mercaptans in Presence of Inorganic Transition Metal Complexes. Indus. Engineer. Ind. Eng. Chem. Process Des. Dev. 1964, 3, 237-241.
Gutteridge, J. M. A. Method for Removal of Trace Iron Contamination from Biological Buffers. FEBS Lett. 1987, 214, 362-364.
Stevens, R.; Stevens, L.; Price, N. C. The Stabilities of Various Thiol Compounds in Protein Purification. Biochem. Educ. 1983, 11, 70.
Spetzler, J. C.; Tam, J. P. Unprotected Peptides as Building Blocks for Branched Peptides and Peptide Dendrimers. Int. J. Pept. Protein Res. 1995, 45, 78-85.
Lees, W. J.; Whitesides, G. M. Equilibrium Constants for Thiol-Disulfide Interchange Reactions: A Coherent, Corrected Set. J. Org. Chem. 1993, 58, 642-647.
Johnson, E. C.; Kent, S. B. H. Insights into the Mechanism and Catalysis of the Native Chemical Ligation Reaction. J. Am. Chem. Soc. 2006, 128, 6640-6646.
Cowper, B.; Sze, T. M.; Premdjee, B.; Bongat White, A. F.; Hacking, A.; Macmillan, D. Examination of Mercaptobenzyl Sulfonates as Catalysts for Native Chemical Ligation: Application to the Assembly of a Glycosylated Glucagon-Like Peptide 1 (GLP-1) Analogue. Chem. Commun. 2015, 51, 3208-3210.
Contreras, J.; Elnagar, A. Y.; Hamm-Alvarez, S. F.; Camarero, J. A. Cellular Uptake of Cyclotide MCoTI-I Follows Multiple Endocytic Pathways. J. Controlled Release 2011, 155, 134-143.
Cleland, W. W. 1, 4-Dithiothreitol. In e-EROS; John Wiley & Sons, Ltd, 2001; DOI: 10. 1002/047084289X. rd473.
Cleland, W. W. Dithiothreitol, a New Protective Reagent for SH Groups. Biochemistry 1964, 3, 480-482.
Guenther, W. H. H. Methods in Selenium Chemistry. III. Reduction of Diselenides with Dithiothreitol. J. Org. Chem. 1967, 32, 3931-3933.
Lambeth, D. O.; Ericson, G. R.; Yorek, M. A.; Ray, P. D. Implications for in Vitro Studies of the Autoxidation of Ferrous Ion and the Iron-Catalyzed Autoxidation of Dithiothreitol. Biochim. Biophys. Acta, Gen. Subj. 1982, 719, 501-508.
Getz, E. B.; Xiao, M.; Chakrabarty, T.; Cooke, R.; Selvin, P. R. A Comparison between the Sulfhydryl Reductants Tris(2-carboxyethyl)phosphine and Dithiothreitol for Use in Protein Biochemistry. Anal. Biochem. 1999, 273, 73-80.
Ruff, Y.; Garavini, V.; Giuseppone, N. Reversible Native Chemical Ligation: A Facile Access to Dynamic Covalent Peptides. J. Am. Chem. Soc. 2014, 136, 6333-6339.
Yost, J. M.; Knight, J. D.; Coltart, D. M. Tris(2-carboxyethyl)-phosphine Hydrochloride. e-EROS 2008, rn00973 DOI: 10. 1002/ 047084289X. rn00973.
Burns, J. A.; Butler, J. C.; Moran, J.; Whitesides, G. M. Selective Reduction of Disulfides by Tris(2-carboxyethyl)phosphine. J. Org. Chem. 1991, 56, 2648-2650.
Pullela, P. K.; Chiku, T.; Carvan, M. J.; Sem, D. S. Fluorescence-Based Detection of Thiols in Vitro and in Vivo Using Dithiol Probes. Anal. Biochem. 2006, 352, 265-273.
Podlaha, J.; Podlahova, J. Compounds Structurally Related to Complexone I. Tris(carboxyethyl)phosphine. Collect. Czech. Chem. Commun. 1973, 38, 1730-1736.
Levison, M. E.; Josephson, A. S.; Kirschenbaum, D. M. Reduction of Biological Substances by Water-Soluble Phosphines: Gamma-Globulin (IgG). Experientia 1969, 25, 126-127.
Gray, W. R. Disulfide Structures of Highly Bridged Peptides: A New Strategy for Analysis. Protein Sci. 1993, 2, 1732-1748.
Cline, D. J.; Redding, S. E.; Brohawn, S. G.; Psathas, J. N.; Schneider, J. P.; Thorpe, C. New Water-Soluble Phosphines as Reductants of Peptide and Protein Disulfide Bonds: Reactivity and Membrane Permeability. Biochemistry 2004, 43, 15195-15203.
Han, J. C.; Han, G. Y. A Procedure for Quantitative Determination of Tris(2-carboxyethyl)phosphine, an Odorless Reducing Agent More Stable and Effective Than. Anal. Biochem. 1994, 220, 5-10.
Faucher, A.-M.; Grand-Maître, C. Tris(2-carboxyethyl)-phosphine (TCEP) for the Reduction of Sulfoxides, Sulfonylchlorides, N-Oxides, and Azides. Synth. Commun. 2003, 33, 3503-3511.
Herbst, E.; Shabat, D. Fret-Based Cyanine Probes for Monitoring Ligation Reactions and their Applications to Mechanistic Studies and Catalyst Screening. Org. Biomol. Chem. 2016, 14, 3715-3728.
Hamm, M. L.; Nikolic, D.; van Breemen, R. B.; Piccirilli, J. A. Unconventional Origin of Metal Ion Rescue in the Hammerhead Ribozyme Reaction: Mn2+-Assisted Redox Conversion of 2'-Mercaptocytidine to Cytidine. J. Am. Chem. Soc. 2000, 122, 12069-12078.
Gorlatov, S. N.; Stadtman, T. C. Human Thioredoxin Reductase from Hela Cells: Selective Alkylation of Selenocysteine in the Protein Inhibits Enzyme Activity and Reduction with NADPH Influences Affinity to Heparin. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 8520-8525.
Metanis, N.; Keinan, E.; Dawson, P. E. Traceless Ligation of Cysteine Peptides Using Selective Deselenization. Angew. Chem., Int. Ed. 2010, 49, 7049-7053.
Muttenthaler, M.; Nevin, S. T.; Grishin, A. A.; Ngo, S. T.; Choy, P. T.; Daly, N. L.; Hu, S. H.; Armishaw, C. J.; Wang, C. I.; Lewis, R. J.; et al. Solving the ?-Conotoxin Folding Problem: Efficient Selenium-Directed on-Resin Generation of More Potent and Stable Nicotinic Acetylcholine Receptor Antagonists. J. Am. Chem. Soc. 2010, 132, 3514-3522.
Walling, C.; Rabinowitz, R. The Reaction of Thiyl Radicals with Trialkyl Phosphites. J. Am. Chem. Soc. 1957, 79, 5326-5326.
Hoffmann, F. W.; Ess, R. J.; Simmons, T. C.; Hanzel, R. S. The Desulfurization of Mercaptans with Trialkyl Phosphites. J. Am. Chem. Soc. 1956, 78, 6414-6414.
Rohde, H.; Schmalisch, J.; Harpaz, Z.; Diezmann, F.; Seitz, O. Ascorbate as an Alternative to Thiol Additives in Native Chemical Ligation. ChemBioChem 2011, 12, 1396-1400.
Fleming, J. E.; Bensch, K. G.; Schreiber, J.; Lohmann, W. Interaction of Ascorbic Acid with Disulfides. Z. Naturforsch., C: J. Biosci. 1983, 38, 859-861.
Giustarini, D.; Dalle-Donne, I.; Colombo, R.; Milzani, A.; Rossi, R. Is Ascorbate Able to Reduce Disulfide Bridges? A Cautionary Note. Nitric Oxide 2008, 19, 252-258.
Forni, L. G.; Monig, J.; Mora-Arellano, V. O.; Willson, R. L. Thiyl Free Radicals: Direct Observations of Electron Transfer Reactions with Phenothiazines and Ascorbate. J. Chem. Soc., Perkin Trans. 2 1983, 2, 961-965.
Bors, W.; Buettner, G. R. The Vitamin C and Its Reactions. In Vitamin C in Health and Disease; Packer, L., Fuchs, J., Eds.; Marcel Dekker, Inc.: New York, 1997, 75-94.
Wintermann, F.; Engelbrecht, S. Reconstitution of the Catalytic Core of F-ATPase ()3? from Escherichia coli Using Chemically Synthesized subunit ?. Angew. Chem., Int. Ed. 2013, 52, 1309-1313.
Isidro-Llobet, A.; álvarez, M.; Albericio, F. Amino Acid-Protecting Groups. Chem. Rev. 2009, 109, 2455-2504.
Canne, L. E.; Figliozzi, G. M.; Robson, B.; Siani, M. A.; Thompson, D. A.; Koike, C.; Tainer, J. A.; Kent, S. B. H.; Simon, R. J. The Total Chemical Synthesis of L-and D-Superoxide Dismutase. Protein Eng. 1997, 10, 23.
Camarero, J. A.; Cotton, G. J.; Adeva, A.; Muir, T. W. Chemical Ligation of Unprotected Peptides Directly from a Solid Support. J. Pept. Res. 1998, 51, 303-316.
Becker, C. F.; Hunter, C. L.; Seidel, R.; Kent, S. B. H.; Goody, R. S.; Engelhard, M. Total Chemical Synthesis of a Functional Interacting Protein Pair: The Protooncogene H-Ras and the Ras-Binding Domain of Its Effector C-Raf1. Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 5075-5080.
Kochendoerfer, G. G.; Chen, S. Y.; Mao, F.; Cressman, S.; Traviglia, S.; Shao, H.; Hunter, C. L.; Low, D. W.; Cagle, E. N.; Carnevali, M.; et al. Design and Chemical Synthesis of a Homogeneous Polymer-Modified Erythropoiesis Protein. Science 2003, 299, 884-887.
Bang, D.; Chopra, N.; Kent, S. B. H. Total Chemical Synthesis of Crambin. J. Am. Chem. Soc. 2004, 126, 1377-1383.
Tesser, G. I.; Balvert-Geers, I. C. The Methylsulfonylethyloxycarbonyl Group, a New and Versatile Amino Protective Function. Int. J. Pept. Protein Res. 1975, 7, 295-305.
Veber, D.; Milkowski, J.; Varga, S.; Denkewalter, R.; Hirschmann, R. Acetamidomethyl. A Novel Thiol Protecting Group for Cysteine. J. Am. Chem. Soc. 1972, 94, 5456-5461.
Bang, D.; Kent, S. B. H. A One-Pot Total Synthesis of Crambin. Angew. Chem., Int. Ed. 2004, 43, 2534-2538.
Canne, L. E.; Botti, P.; Simon, R. J.; Chen, Y.; Dennis, E. A.; Kent, S. B. H. Chemical Protein Synthesis by Solid Phase Ligation of Unprotected Peptide Segments. J. Am. Chem. Soc. 1999, 121, 8720-8727.
Johnson, E. C.; Durek, T.; Kent, S. B. H. Total Chemical Synthesis, Folding, and Assay of a Small Protein on a Water-Compatible Solid Support. Angew. Chem., Int. Ed. 2006, 45, 3283-3287.
Jbara, M.; Seenaiah, M.; Brik, A. Solid Phase Chemical Ligation Employing a Rink Amide Linker for the Synthesis of Histone H2B Protein. Chem. Commun. 2014, 50, 12534-12537.
Wheelan, S. J.; Marchler-Bauer, A.; Bryant, S. H. Domain Size Distributions Can Predict Domain Boundaries. Bioinformatics 2000, 16, 613-618.
Piontek, C.; Varon Silva, D.; Heinlein, C.; Pohner, C.; Mezzato, S.; Ring, P.; Martin, A.; Schmid, F. X.; Unverzagt, C. Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C: Part 2. Angew. Chem., Int. Ed. 2009, 48, 1941-1945.
Maity, S. K.; Jbara, M.; Laps, S.; Brik, A. Efficient Palladium-Assisted One-Pot Deprotection of (Acetamidomethyl)Cysteine Following Native Chemical Ligation and/or Desulfurization to Expedite Chemical Protein Synthesis. Angew. Chem., Int. Ed. 2016, 55, 8108-8112.
Jbara, M.; Maity, S. K.; Seenaiah, M.; Brik, A. Palladium Mediated Rapid Deprotection of N-Terminal Cysteine under Native Chemical Ligation Conditions for the Efficient Preparation of Synthetically Challenging Proteins. J. Am. Chem. Soc. 2016, 138, 5069-5075.
Jbara, M.; Laps, S.; Morgan, M.; Kamnesky, G.; Mann, G.; Wolberger, C.; Brik, A. Palladium Prompted on-Demand Cysteine Chemistry for the Synthesis of Challenging and Uniquely Modified Proteins. Nat. Commun. 2018, 9, 3154.
Maity, S. K.; Jbara, M.; Mann, G.; Kamnesky, G.; Brik, A. Total Chemical Synthesis of Histones and their Analogs, Assisted by Native Chemical Ligation and Palladium Complexes. Nat. Protoc. 2017, 12, 2293-2322.
Di Bello, C.; Filira, F.; Giormani, V.; D'Angeli, F. An Investigation of Racemisation During the Use of Acetoacetyl-L-Valine in Peptide Synthesis. J. Chem. Soc. C 1969, 350-352.
D'Angeli, F.; Filira, F.; Scoffone, E. The Acetoacetyl Group, an Amino Protective Group of Potential Use in Peptide Synthesis. Tetrahedron Lett. 1965, 6, 605-608.
Boll, E.; Ebran, J. P.; Drobecq, H.; El-Mahdi, O.; Raibaut, L.; Ollivier, N.; Melnyk, O. Access to Large Cyclic Peptides by a One-Pot Two-Peptide Segment Ligation/Cyclization Process. Org. Lett. 2015, 17, 130-133.
Tang, S.; Si, Y.-Y.; Wang, Z.-P.; Mei, K.-R.; Chen, X.; Cheng, J.-Y.; Zheng, J.-S.; Liu, L. An Efficient One-Pot Four-Segment Condensation Method for Protein Chemical Synthesis. Angew. Chem., Int. Ed. 2015, 54, 5713-5717.
Loibl, S. F.; Harpaz, Z.; Zitterbart, R.; Seitz, O. Total Chemical Synthesis of Proteins without HPLC Purification. Chem. Sci. 2016, 7, 6753-6759.
Yang, Y. Y.; Ficht, S.; Brik, A.; Wong, C. H. Sugar-Assisted Ligation in Glycoprotein Synthesis. J. Am. Chem. Soc. 2007, 129, 7690-7701.
Sato, K.; Kitakaze, K.; Nakamura, T.; Naruse, N.; Aihara, K.; Shigenaga, A.; Inokuma, T.; Tsuji, D.; Itoh, K.; Otaka, A. The Total Chemical Synthesis of the Monoglycosylated GM2 Ganglioside Activator Using a Novel Cysteine Surrogate. Chem. Commun. 2015, 51, 9946-9948.
Harpaz, Z.; Siman, P.; Kumar, K. S.; Brik, A. Protein Synthesis Assisted by Native Chemical Ligation at Leucine. ChemBioChem 2010, 11, 1232-1235.
Far, S.; Melnyk, O. Synthesis of Glyoxylyl Peptides Using a Phosphine Labile-Diaminoacetic Acid Derivative. Tetrahedron Lett. 2004, 45, 7163-7165.
Far, S.; Gouyette, C.; Melnyk, O. A Novel Phosphoramidite for the Synthesis of ?-Oxo Aldehyde-Modified Oligodeoxynucleotides. Tetrahedron 2005, 61, 6138-6142.
Dong, S.; Shang, S.; Tan, Z.; Danishefsky, S. J. Toward Homogeneous Erythropoietin: Application of Metal-Free Dethiylation in the Chemical Synthesis of the Ala79-Arg166 Glycopeptide Domain. Isr. J. Chem. 2011, 51, 968-976.
Huang, Y.-C.; Chen, C.-C.; Gao, S.; Wang, Y.-H.; Xiao, H.; Wang, F.; Tian, C.-L.; Li, Y.-M. Synthesis of L-and D-Ubiquitin by One-Pot Ligation and Metal-Free Desulfurization. Chem.-Eur. J. 2016, 22, 7623-7628.
Pool, C. T.; Boyd, J. G.; Tam, J. P. Ninhydrin as a Reversible Protecting Group of Amino-Terminal Cysteine. J. Pept. Res. 2004, 63, 223-234.
Smith, A. B.; Savinov, S. N.; Manjappara, U. V.; Chaiken, I. M. Peptide-Small Molecule Hybrids via Orthogonal Deprotection-Chemoselective Conjugation to Cysteine-Anchored Scaffolds. A Model Study. Org. Lett. 2002, 4, 4041-4044.
Piontek, C.; Ring, P.; Harjes, O.; Heinlein, C.; Mezzato, S.; Lombana, N.; Pohner, C.; Puttner, M.; Varon Silva, D.; Martin, A.; et al. Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C: Part 1. Angew. Chem., Int. Ed. 2009, 48, 1936-1940.
Pan, M.; He, Y.; Wen, M.; Wu, F.; Sun, D.; Li, S.; Zhang, L.; Li, Y.; Tian, C. One-Pot Hydrazide-Based Native Chemical Ligation for Efficient Chemical Synthesis and Structure Determination of Toxin Mambalgin-1. Chem. Commun. 2014, 50, 5837-5839.
Mochizuki, M.; Hibino, H.; Nishiuchi, Y. Postsynthetic Modification of Unprotected Peptides via S-Tritylation Reaction. Org. Lett. 2014, 16, 5740-5743.
Pentelute, B. L.; Kent, S. B. H. Selective Desulfurization of Cysteine in the Presence of Cys(Acm) in Polypeptides Obtained by Native Chemical Ligation. Org. Lett. 2007, 9, 687-690.
Shen, F.; Zhang, Z. P.; Li, J. B.; Lin, Y.; Liu, L. Hydrazine-Sensitive Thiol Protecting Group for Peptide and Protein Chemistry. Org. Lett. 2011, 13, 568-571.
Siman, P.; Blatt, O.; Moyal, T.; Danieli, T.; Lebendiker, M.; Lashuel, H. A.; Friedler, A.; Brik, A. Chemical Synthesis and Expression of the HIV-1 Rev Protein. ChemBioChem 2011, 12, 1097-1104.
Saporito, A.; Marasco, D.; Chambery, A.; Botti, P.; Monti, S. M.; Pedone, C.; Ruvo, M. The Chemical Synthesis of the GstI Protein by NCL on a X-Met Site. Biopolymers 2006, 83, 508-518.
Katayama, H.; Nakahara, Y.; Hojo, H. N-Methyl-Phenacyloxycarbamidomethyl (Pocam) Group: A Novel Thiol Protecting Group for Solid-Phase Peptide Synthesis and Peptide Condensation Reactions. Org. Biomol. Chem. 2011, 9, 4653-4661.
Qi, Y. K.; Tang, S.; Huang, Y. C.; Pan, M.; Zheng, J. S.; Liu, L. Hmb(off/on) as a Switchable Thiol Protecting Group for Native Chemical Ligation. Org. Biomol. Chem. 2016, 14, 4194-4198.
Gieselman, M. D.; Xie, L.; van Der Donk, W. A. Synthesis of a Selenocysteine-Containing Peptide by Native Chemical Ligation. Org. Lett. 2001, 3, 1331-1334.
Quaderer, R.; Sewing, A.; Hilvert, D. Selenocysteine-Mediated Native Chemical Ligation. Helv. Chim. Acta 2001, 84, 1197-1206.
Hondal, R. J.; Nilsson, B. L.; Raines, R. T. Selenocysteine in Native Chemical Ligation and Expressed Protein Ligation. J. Am. Chem. Soc. 2001, 123, 5140-5141.
Reich, H. J.; Hondal, R. J. Why Nature Chose Selenium. ACS Chem. Biol. 2016, 11, 821-841.
Muttenthaler, M.; Alewood, P. F. Selenopeptide Chemistry. J. Pept. Sci. 2008, 14, 1223-1239.
Malins, L. R.; Mitchell, N. J.; Payne, R. J. Peptide Ligation Chemistry at Selenol Amino Acids. J. Pept. Sci. 2014, 20, 64-77.
Mobli, M.; Morgenstern, D.; King, G. F.; Alewood, P. F.; Muttenthaler, M. Site-Specific pKa Determination of Selenocysteine Residues in Selenovasopressin by Using 77Se NMR Spectroscopy. Angew. Chem., Int. Ed. 2011, 50, 11952-11955.
Huber, R. E.; Criddle, R. S. Comparison of the Chemical Properties of Selenocysteine and Selenocystine with their Sulfur Analogs. Arch. Biochem. Biophys. 1967, 122, 164-173.
Dery, S.; Reddy, P. S.; Dery, L.; Mousa, R.; Dardashti, R. N.; Metanis, N. Insights into the Deselenization of Selenocysteine into Alanine and Serine. Chem. Sci. 2015, 6, 6207-6212.
Ollivier, N.; Blanpain, A.; Boll, E.; Raibaut, L.; Drobecq, H.; Melnyk, O. Selenopeptide Transamidation and Metathesis. Org. Lett. 2014, 16, 4032-4035.
Shimodaira, S.; Takei, T.; Hojo, H.; Iwaoka, M. Synthesis of Selenocysteine-Containing Cyclic Peptides via Tandem N-to-S Acyl Migration and Intramolecular Selenocysteine-Mediated Native Chemical Ligation. Chem. Commun. 2018, 54, 11737-11740.
Reddy, P. S.; Dery, S.; Metanis, N. Chemical Synthesis of Proteins with Non-Strategically Placed Cysteines Using Selenazolidine and Selective Deselenization. Angew. Chem., Int. Ed. 2016, 55, 992-995.
Schwyzer, R.; Coenzym, A. Modellversuche zur Biologischen Acylierungsreaktion. Uber die Reaktionsfáhigkeit von Thiolcarbonsáuren und ihren Estern. Helv. Chim. Acta 1953, 36, 414-424.
Farrington, J. A.; Hextall, P. J.; Kenner, G. W.; Turner, J. M. 265. Peptides. Part VII. The Preparation and Use of p-Nitrophenyl Thiolesters. J. Chem. Soc. 1957, 1407-1413.
Kenner, G. W.; Thomson, P. J.; Turner, J. M. 835. Peptides. Part VIII. Cyclic Peptides Derived from Leucine and Glycine. J. Chem. Soc. 1958, 4148-4152.
Shalitin, Y.; Bernhard, S. A. Neighboring Group Effects on Ester Hydrolysis. I. Neighboring Hydroxyl Groups. J. Am. Chem. Soc. 1964, 86, 2291-2292.
Lloyd, K.; Young, G. T. The Use of Acylamino-Acid Esters of 2-Mercaptopyridine in Peptide Synthesis. Chem. Commun. 1968, 1400b-1401.
Jakubke, H. D. Uber Aktivierte Ester Peptidsynthese mit NAcylaminosáure-8-Thiochinolylestern. Z. Chem. 1965, 5, 453-454.
Lloyd, K.; Young, G. T. Amino-Acids and Peptides. Part XXXIV. Anchimerically Assisted Coupling Reactions: The Use of 2-Pyridyl Thiolesters. J. Chem. Soc. C 1971, 2890-2896.
Ueda, M.; Sato, A.; Imai, Y. Synthesis of Polyamides from Active 2-Benzothiazolyl Dithiolesters and Diamines under Mild Conditions. J. Polym. Sci., Polym. Chem. Ed. 1978, 16, 475-482.
Davis, A. P.; Walsh, J. J. Amide Bond Formation via Pentafluorothiophenyl Active Esters. Tetrahedron Lett. 1994, 35, 4865-4868.
Ishiwata, A.; Ichiyanagi, T.; Takatani, M.; Ito, Y. Chemoselective Peptide Bond Formation Using Formyl-Substituted Nitrophenylthio Ester. Tetrahedron Lett. 2003, 44, 3187-3190.
Durek, T.; Torbeev, V. Y.; Kent, S. B. H. Convergent Chemical Synthesis and High-Resolution X-Ray Structure of Human Lysozyme. Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 4846-4851.
Torbeev, V. Y.; Kent, S. B. H. Convergent Chemical Synthesis and Crystal Structure of a 203 Amino Acid "Covalent Dimer" HIV-1 Protease Enzyme Molecule. Angew. Chem., Int. Ed. 2007, 46, 1667-1670.
Banigan, J. R.; Mandal, K.; Sawaya, M. R.; Thammavongsa, V.; Hendrickx, A. P.; Schneewind, O.; Yeates, T. O.; Kent, S. B. H. Determination of the X-Ray Structure of the Snake Venom Protein Omwaprin by Total Chemical Synthesis and Racemic Protein Crystallography. Protein Sci. 2010, 19, 1840-1849.
Mandal, K.; Pentelute, B. L.; Bang, D.; Gates, Z. P.; Torbeev, V. Y.; Kent, S. B. H. Design, Total Chemical Synthesis, and X-Ray Structure of a Protein Having a Novel Linear-Loop Polypeptide Chain Topology. Angew. Chem., Int. Ed. 2012, 51, 1481-1486.
Castro, E. A. Kinetics and Mechanisms of Reactions of Thiol, Thiono, and Dithio Analogues of Carboxylic Esters with Nucleophiles. Chem. Rev. 1999, 99, 3505-3524.
Dawson, P. E.; Churchill, M. J.; Ghadiri, M. R.; Kent, S. B. H. Modulation of Reactivity in Native Chemical Ligation through the Use of Thiol Additives. J. Am. Chem. Soc. 1997, 119, 4325-4329.
van de Langemheen, H.; Brouwer, A. J.; Kemmink, J.; Kruijtzer, J. A. W.; Liskamp, R. M. J. Synthesis of Cyclic Peptides Containing a Thioester Handle for Native Chemical Ligation. J. Org. Chem. 2012, 77, 10058-10064.
Campopiano, O.; Minassian, F. Thiophenol. In e-EROS; John Wiley & Sons, Ltd, 2001; DOI: 10. 1002/047084289X. rt101. pub2.
Ayres, D.; Hellier, D. Dictionary of Environmentaly Important Chemicals; Chapman & Hall: London, 1998.
DeCollo, T. V.; Lees, W. J. Effects of Aromatic Thiols on Thiol-Disulfide Interchange Reactions That Occur During Protein Folding. J. Org. Chem. 2001, 66, 4244-4249.
Wang, C.; Guo, Q.-X.; Fu, Y. Theoretical Analysis of the Detailed Mechanism of Native Chemical Ligation Reactions. Chem.-Asian J. 2011, 6, 1241-1251.
Sun, X.-H.; Yu, H.-Z.; Pei, S.-Q.; Dang, Z.-M. Theoretical Investigations on the Thiol-Thioester Exchange Steps of Different Thioesters. Chin. Chem. Lett. 2015, 26, 1259-1264.
Gentle, I. E.; De Souza, D. P.; Baca, M. Direct Production of Proteins with N-Terminal Cysteine for Site-Specific Conjugation. Bioconjugate Chem. 2004, 15, 658-663.
Lahiri, S.; Brehs, M.; Olschewski, D.; Becker, C. F. Total Chemical Synthesis of an Integral Membrane Enzyme: Diacylglycerol Kinase from Escherichia coli. Angew. Chem., Int. Ed. 2011, 50, 3988-3992.
Jencks, W. P.; Salvesen, K. Equilibrium Deuterium Isotope Effects on the Ionization of Thiol Acids. J. Am. Chem. Soc. 1971, 93, 4433-4436.
Gregory, M. J.; Bruice, T. C. Nucleophilic Displacement Reactions at the Thiol Ester Bond. V. Reactions of 2, 2, 2-Trifluoroethyl Thiolacetate. J. Am. Chem. Soc. 1967, 89, 2121-2127.
Heller, M. J.; Walder, J. A.; Klotz, I. M. Intramolecular Catalysis of Acylation and Deacylation in Peptides Containing Cysteine and Histidine. J. Am. Chem. Soc. 1977, 99, 2780-2785.
Tsuda, S.; Yoshiya, T.; Mochizuki, M.; Nishiuchi, Y. Synthesis of Cysteine-Rich Peptides by Native Chemical Ligation without Use of Exogenous Thiols. Org. Lett. 2015, 17, 1806-1809.
Tsuda, S.; Mochizuki, M.; Nishio, H.; Yoshiya, T.; Nishiuchi, Y. Development of a Sufficiently Reactive Thioalkylester Involving the Side-Chain Thiol of Cysteine Applicable for Kinetically Controlled Ligation. Biopolymers 2016, 106, 503-511.
Schmalisch, J.; Seitz, O. Acceleration of Thiol Additive-Free Native Chemical Ligation by Intramolecular S-> S Acyl Transfer. Chem. Commun. 2015, 51, 7554-7557.
Bender, M. L.; Turnquest, B. W. General Basic Catalysis of Ester Hydrolysis and Its Relationship to Enzymatic Hydrolysis. J. Am. Chem. Soc. 1957, 79, 1656-1662.
Fedor, L. R.; Bruice, T. C. Nucleophilic Displacement Reactions at the Thiolester Bond. II. Hydrazinolysis and Morpholinolysis in Aqueous Solution. J. Am. Chem. Soc. 1964, 86, 4117-4123.
Li, Y.; Yongye, A.; Giulianotti, M.; Martinez-Mayorga, K.; Yu, Y.; Houghten, R. A. Synthesis of Cyclic Peptides through Direct Aminolysis of Peptide Thioesters Catalyzed by Imidazole in Aqueous Organic Solutions. J. Comb. Chem. 2009, 11, 1066-1072.
Li, Y.; Giulionatti, M.; Houghten, R. A. Macrolactonization of Peptide Thioesters Catalyzed by Imidazole and Its Application in the Synthesis of Kahalalide B and Analogues. Org. Lett. 2010, 12, 2250-2253.
Sakamoto, K.; Tsuda, S.; Mochizuki, M.; Nohara, Y.; Nishio, H.; Yoshiya, T. Imidazole-Aided Native Chemical Ligation: Imidazole as a One-Pot Desulfurization-Amenable Non-Thiol-Type Alternative to 4-Mercaptophenylacetic Acid. Chem.-Eur. J. 2016, 22, 17940-17944.
Sakamoto, K.; Tsuda, S.; Nishio, H.; Yoshiya, T. 1, 2, 4-Triazole-Aided Native Chemical Ligation between Peptide-N-Acyl-N'-Methyl-Benzimidazolinone and Cysteinyl Peptide. Chem. Commun. 2017, 53, 12236-12239.
Chisholm, T. S.; Clayton, D.; Dowman, L. J.; Sayers, J.; Payne, R. J. Native Chemical Ligation-Photodesulfurization in Flow. J. Am. Chem. Soc. 2018, 140, 9020-9024.
Zhang, L.; Tam, J. P. Orthogonal Coupling of Unprotected Peptide Segments through Histidyl Amino Terminus. Tetrahedron Lett. 1997, 38, 3-6.
Vedejs, E.; Diver, S. T. Tributylphosphine: A Remarkable Acylation Catalyst. J. Am. Chem. Soc. 1993, 115, 3358-3359.
Vedejs, E.; Bennett, N. S.; Conn, L. M.; Diver, S. T.; Gingras, M.; Lin, S.; Oliver, P. A.; Peterson, M. J. Tributylphosphine-Catalyzed Acylations of Alcohols: Scope and Related Reactions. J. Org. Chem. 1993, 58, 7286-7288.
Huang, J.; Li, C.; Nolan, S. P.; Petersen, J. L. Solution Calorimetric Investigation of Oxidative Addition of HEAr (E = O, S, Se; Ar = C6H4X, X = CH3, H, Cl, NO2) to (PMe3)4Ru(C2H4): Relationship between HEAr Acidity and Enthalpy of Reaction. Organometallics 1998, 17, 3516-3521.
Thapa, B.; Schlegel, H. B. Theoretical Calculation of pKa's of Selenols in Aqueous Solution Using an Implicit Solvation Model and Explicit Water Molecules. J. Phys. Chem. A 2016, 120, 8916-8922.
Fagioli, F.; Pulidori, F.; Bighi, C.; De Battisti, A. Polarographic Reduction of Diphenyldiselenide at DME. Gazz. Chim. Ital. 1974, 104, 639-647.
Reich, H. J.; Cohen, M. L. Organoselenium Chemistry. Dealkylation of Amines with Benzeneselenol. J. Org. Chem. 1979, 44, 3148-3151.
Bang, D.; Pentelute, B. L.; Kent, S. B. H. Kinetically Controlled Ligation for the Convergent Chemical Synthesis of Proteins. Angew. Chem., Int. Ed. 2006, 45, 3985-3988.
Nakamura, T.; Shigenaga, A.; Sato, K.; Tsuda, Y.; Sakamoto, K.; Otaka, A. Examination of Native Chemical Ligation Using Peptidyl Prolyl Thioesters. Chem. Commun. 2014, 50, 58-60.
Liu, S.; Pentelute, B. L.; Kent, S. B. H. Convergent Chemical Synthesis of [Lysine(24, 38, 83)] Human Erythropoietin. Angew. Chem., Int. Ed. 2012, 51, 993-999.
Lee, J.; Kwon, Y.; Pentelute, B. L.; Bang, D. Use of Model Peptide Reactions for the Characterization of Kinetically Controlled Ligation. Bioconjugate Chem. 2011, 22, 1645-1649.
Lee, D. H.; Granja, J. R.; Martinez, J. A.; Severin, K.; Ghadiri, M. R. A Self-Replicating Peptide. Nature 1996, 382, 525-528.
Yao, S.; Ghosh, I.; Zutshi, R.; Chmielewski, J. A pHModulated, Self-Replicating Peptide. J. Am. Chem. Soc. 1997, 119, 10559-10560.
Rubinov, B.; Wagner, N.; Rapaport, H.; Ashkenasy, G. Self-Replicating Amphiphilic Beta-Sheet Peptides. Angew. Chem., Int. Ed. 2009, 48, 6683-6686.
Erben, A.; Grossmann, T. N.; Seitz, O. DNA-Triggered Synthesis and Bioactivity of Proapoptotic Peptides. Angew. Chem., Int. Ed. 2011, 50, 2828-2832.
Erben, A.; Grossmann, T. N.; Seitz, O. DNA-Instructed Acyl Transfer Reactions for the Synthesis of Bioactive Peptides. Bioorg. Med. Chem. Lett. 2011, 21, 4993-4997.
Grossmann, T. N.; Roglin, L.; Seitz, O. Target-Catalyzed Transfer Reactions for the Amplified Detection of RNA. Angew. Chem., Int. Ed. 2008, 47, 7119-7122.
Grossmann, T. N.; Seitz, O. DNA-Catalyzed Transfer of a Reporter Group. J. Am. Chem. Soc. 2006, 128, 15596-15597.
Sayers, J.; Payne, R. J.; Winssinger, N. Peptide Nucleic Acid-Templated Selenocystine-Selenoester Ligation Enables Rapid miRNA Detection. Chem. Sci. 2018, 9, 896-903.
Middel, S.; Panse, C. H.; Nawratil, S.; Diederichsen, U. Native Chemical Ligation Directed by Photocleavable Peptide Nucleic Acid (PNA) Templates. ChemBioChem 2017, 18, 2328-2332.
Beligere, G. S.; Dawson, P. E. Conformationally Assisted Protein Ligation Using C-Terminal Thioester Peptides. J. Am. Chem. Soc. 1999, 121, 6332-6333.
Zhao, L.; Ehrt, C.; Koch, O.; Wu, Y. W. One-Pot N2C/C2C/ N2N Ligation to Trap Weak Protein-Protein Interactions. Angew. Chem., Int. Ed. 2016, 55, 8129-8133.
Litowski, J. R.; Hodges, R. S. Designing Heterodimeric Two-Stranded Alpha-Helical Coiled-Coils. Effects of Hydrophobicity and Alpha-Helical Propensity on Protein Folding, Stability, and Specificity. J. Biol. Chem. 2002, 277, 37272-37279.
Tian, H.; FUrstenberg, A.; Huber, T. Labeling and Single-Molecule Methods to Monitor G Protein-Coupled Receptor Dynamics. Chem. Rev. 2017, 117, 186-245.
Reinhardt, U.; Lotze, J.; Morl, K.; Beck-Sickinger, A. G.; Seitz, O. Rapid Covalent Fluorescence Labeling of Membrane Proteins on Live Cells via Coiled-Coil Templated Acyl Transfer. Bioconjugate Chem. 2015, 26, 2106-2117.
Lotze, J.; Reinhardt, U.; Seitz, O.; Beck-Sickinger, A. G. Peptide-Tags for Site-Specific Protein Labelling in Vitro and in Vivo. Mol. BioSyst. 2016, 12, 1731-1745.
Zheng, J.-S.; Tang, S.; Guo, Y.; Chang, H.-N.; Liu, L. Synthesis of Cyclic Peptides and Cyclic Proteins via Ligation of Peptide Hydrazides. ChemBioChem 2012, 13, 542-546.
Tam, J. P.; Lu, Y. A. A Biomimetic Strategy in the Synthesis and Fragmentation of Cyclic Protein. Protein Sci. 1998, 7, 1583-1592.
Ollivier, N.; Toupy, T.; Hartkoorn, R. C.; Desmet, R.; Monbaliu, J.-C. M.; Melnyk, O. Accelerated Microfluidic Native Chemical Ligation at Difficult Amino Acids toward Cyclic Peptides. Nat. Commun. 2018, 9, 2847.
Mulvenna, J. P.; Wang, C.; Craik, D. J. Cybase: A Database of Cyclic Protein Sequence and Structure. Nucleic Acids Res. 2006, 34, D192-D194.
Aragón, E.; Goerner, N.; Xi, Q.; Gomes, T.; Gao, S.; Massagué, J.; Massagué, M. J. Structural Basis for the Versatile Interactions of Smad7 with Regulator WW Domains in TGF-? Pathways. Structure 2012, 20, 1726-1736.
Stirling, C. J. M. 913. Thiol-Esters. Part II. The Chlorination of 2-Diethylaminoethyl Thiolbenzoate and the Rearrangement of 2-Alkylaminoethyl Thiolbenzoates. J. Chem. Soc. 1958, 4524-4530.
Wieland, T.; Lang, H. U.; Liebsch, D. Uber Peptidsynthesen. 11. Mitteilung. Intramolekulare Aminoacylwanderung bei Peptiden. Liebigs Ann. Chem. 1955, 597, 227-234.
Wieland, T.; Hornig, H. S-Acylspaltung bei S-Acetyl-?-aminomercaptanen Verschiedener Kettenlánge. Liebigs Ann. Chem. 1956, 600, 12-22.
Cuccovia, I. M.; Schroeter, E. H.; De Baptista, R. C.; Chaimovich, H. Effect of Detergents on the S-to N-Acyl Transfer of S-acyl-?-mercaptoethylamines. J. Org. Chem. 1977, 42, 3400-3403.
Trudelle, Y.; Caille, A. Reactivity of Sulfhydryl Group in Peptides and Polypeptides with p-Nitrophenylacetate. S to N Acyl Shift in Cysteine. Int. J. Pept. Protein Res. 1977, 10, 291-298.
Sheradsky, T. Rearrangements Involving Thiols. In The Thiol Group (1974); John Wiley & Sons, Ltd., 1974; pp 685-719.
Martin, R. B.; Hedrick, R. I.; Parcell, A. Thiazoline and Oxazoline Hydrolyses and Sulfur-Nitrogen and Oxygen-Nitrogen Acyl Transfer Reactions. J. Org. Chem. 1964, 29, 3197-3206.
Satterthwait, A. C.; Jencks, W. P. Mechanism of the Aminolysis of Acetate Esters. J. Am. Chem. Soc. 1974, 96, 7018-7031.
Zipse, H.; Wang, L.-H.; Houk, K. N. Polyether Catalysis of Ester Aminolysis-a Computational and Experimental Study. Liebigs Ann. 1996, 1996, 1511-1522.
Singleton, D. A.; Merrigan, S. R. Resolution of Conflicting Mechanistic Observations in Ester Aminolysis. A Warning on the Qualitative Prediction of Isotope Effects for Reactive Intermediates. J. Am. Chem. Soc. 2000, 122, 11035-11036.
Ilieva, S.; Galabov, B.; Musaev, D. G.; Morokuma, K.; Schaefer, H. F. Computational Study of the Aminolysis of Esters. The Reaction of Methylformate with Ammonia. J. Org. Chem. 2003, 68, 1496-1502.
Martin, R. B.; Lowey, S.; Elson, E. L.; Edsall, J. T. Hydrolysis of 2-Methyl-?2-Thiazoline and Its Formation from N-acetyl-?-mercaptoethylamine. Observations on an N-S Acyl Shift. J. Am. Chem. Soc. 1959, 81, 5089-5095.
Martin, R. B.; Parcell, A. Hydrolysis of 2-Substituted ?2-Thiazolines. J. Am. Chem. Soc. 1961, 83, 4830-4834.
Barnett, R.; Jencks, W. P. Rate-Limiting Diffusion-Controlled Proton Transfer in an Acetyl Transfer Reaction. J. Am. Chem. Soc. 1968, 90, 4199-4200.
Macmillan, D.; De Cecco, M.; Reynolds, N. L.; Santos, L. F. A.; Barran, P. E.; Dorin, J. R. Synthesis of Cyclic Peptides through an Intramolecular Amide Bond Rearrangement. ChemBioChem 2011, 12, 2133-2136.
Adams, A. L.; Macmillan, D. Investigation of Peptide Thioester Formation via N->Se Acyl Transfer. J. Pept. Sci. 2013, 19, 65-73.
Kryukov, G. V.; Castellano, S.; Novoselov, S. V.; Lobanov, A. V.; Zehtab, O.; Guigó, R.; Gladyshev, V. N. Characterization of Mammalian Selenoproteomes. Science 2003, 300, 1439-1443.
Dery, L.; Reddy, P. S.; Dery, S.; Mousa, R.; Ktorza, O.; Talhami, A.; Metanis, N. Accessing Human Selenoproteins through Chemical Protein Synthesis. Chem. Sci. 2017, 8, 1922-1926.
Liu, J.; Cheng, R.; Rozovsky, S. Synthesis and Semisynthesis of Selenopeptides and Selenoproteins. Curr. Opin. Chem. Biol. 2018, 46, 41-47.
Besse, D.; Budisa, N.; Karnbrock, W.; Minks, C.; Musiol, H. J.; Pegoraro, S.; Siedler, F.; Weyher, E.; Moroder, L. Chalcogen-Analogs of Amino Acids. Their Use in X-Ray Crystallographic and Folding Studies of Peptides and Proteins. Biol. Chem. 1997, 378, 211-218.
Casi, G.; Roelfes, G.; Hilvert, D. Selenoglutaredoxin as a Glutathione Peroxidase Mimic. ChemBioChem 2008, 9, 1623-1631.
Metanis, N.; Keinan, E.; Dawson, P. E. Synthetic Seleno-Glutaredoxin 3 Analogues Are Highly Reducing Oxidoreductases with Enhanced Catalytic Efficiency. J. Am. Chem. Soc. 2006, 128, 16684-16691.
Muttenthaler, M.; Andersson, A.; Vetter, I.; Menon, R.; Busnelli, M.; Ragnarsson, L.; Bergmayr, C.; Arrowsmith, S.; Deuis, J. R.; Chiu, H. S.; et al. Subtle Modifications to Oxytocin Produce Ligands That Retain Potency and Improved Selectivity across Species. Sci. Signaling 2017, 10, No. eaan3398.
Muttenthaler, M.; Andersson, A.; de Araujo, A. D.; Dekan, Z.; Lewis, R. J.; Alewood, P. F. Modulating Oxytocin Activity and Plasma Stability by Disulfide Bond Engineering. J. Med. Chem. 2010, 53, 8585-8596.
Pegoraro, S.; Fiori, S.; Cramer, J.; Rudolph-Bohner, S.; Moroder, L. The Disulfide-Coupled Folding Pathway of Apamin as Derived from Diselenide-Quenched Analogs and Intermediates. Protein Sci. 1999, 8, 1605-1613.
Metanis, N.; Hilvert, D. Harnessing Selenocysteine Reactivity for Oxidative Protein Folding. Chem. Sci. 2015, 6, 322-325.
Muttenthaler, M.; Nevin, S. T.; Grishin, A. A.; Ngo, S. T.; Choy, P. T.; Daly, N. L.; Hu, S. H.; Armishaw, C. J.; Wang, C. I.; Lewis, R. J.; et al. Solving the Alpha-Conotoxin Folding Problem: Efficient Selenium-Directed on-Resin Generation of More Potent and Stable Nicotinic Acetylcholine Receptor Antagonists. J. Am. Chem. Soc. 2010, 132, 3514-3522.
de Araujo, A. D.; Callaghan, B.; Nevin, S. T.; Daly, N. L.; Craik, D. J.; Moretta, M.; Hopping, G.; Christie, M. J.; Adams, D. J.; Alewood, P. F. Total Synthesis of the Analgesic Conotoxin MrVIB through Selenocysteine-Assisted Folding. Angew. Chem., Int. Ed. 2011, 50, 6527-6529.
Mousa, R.; Notis Dardashti, R.; Metanis, N. Selenium and Selenocysteine in Protein Chemistry. Angew. Chem., Int. Ed. 2017, 56, 15818-15827.
Craik, D. J. Protein Folding: Turbo-Charged Crosslinking. Nat. Chem. 2012, 4, 600-602.
Besse, D.; Moroder, L. Synthesis of Selenocysteine Peptides and their Oxidation to Diselenide-Bridged Compounds. J. Pept. Sci. 1997, 3, 442-453.
Harris, K. M.; Flemer, S., Jr.; Hondal, R. J. Studies on Deprotection of Cysteine and Selenocysteine Side-Chain Protecting Groups. J. Pept. Sci. 2007, 13, 81-93.
Malins, L. R.; Mitchell, N. J.; McGowan, S.; Payne, R. J. Oxidative Deselenization of Selenocysteine: Applications for Programmed Ligation at Serine. Angew. Chem., Int. Ed. 2015, 54, 12716-12721.
Mitchell, N. J.; Kulkarni, S. S.; Malins, L. R.; Wang, S.; Payne, R. J. One-Pot Ligation-Oxidative Deselenization at Selenocysteine and Selenocystine. Chem.-Eur. J. 2017, 23, 946-952.
Melnyk, O.; Agouridas, V. From Protein Total Synthesis to Peptide Transamidation and Metathesis: Playing with the Reversibility of N, S-Acyl or N, Se-Acyl Migration Reactions. Curr. Opin. Chem. Biol. 2014, 22, 137-145.
Ohta, Y.; Itoh, S.; Shigenaga, A.; Shintaku, S.; Fujii, N.; Otaka, A. Cysteine-Derived S-Protected Oxazolidinones: Potential Chemical Devices for the Preparation of Peptide Thioesters. Org. Lett. 2006, 8, 467-470.
Hou, W.; Zhang, X.; Li, F.; Liu, C. F. Peptidyl N, N-Bis(2-Mercaptoethyl)-Amides as Thioester Precursors for Native Chemical Ligation. Org. Lett. 2011, 13, 386-389.
Sato, K.; Shigenaga, A.; Tsuji, K.; Tsuda, S.; Sumikawa, Y.; Sakamoto, K.; Otaka, A. N-Sulfanylethylanilide Peptide as a Crypto-Thioester Peptide. ChemBioChem 2011, 12, 1840-1844.
Burlina, F.; Papageorgiou, G.; Morris, C.; White, P. D.; Offer, J. In Situ Thioester Formation for Protein Ligation Using ?-Methylcysteine. Chem. Sci. 2014, 5, 766-770.
Terrier, V. P.; Adihou, H.; Arnould, M.; Delmas, A. F.; Aucagne, V. A Straightforward Method for Automated Fmoc-Based Synthesis of Bio-Inspired Peptide Crypto-Thioesters. Chem. Sci. 2016, 7, 339-345.
Desmet, R.; Pauzuolis, M.; Boll, E.; Drobecq, H.; Raibaut, L.; Melnyk, O. Synthesis of Unprotected Linear or Cyclic O-Acyl Isopeptides in Water Using Bis(2-Sulfanylethyl)Amido Peptide Ligation. Org. Lett. 2015, 17, 3354-3357.
Kawakami, T.; Aimoto, S. The Use of a Cysteinyl Prolyl Ester (CPE) Autoactivating Unit in Peptide Ligation Reactions. Tetrahedron 2009, 65, 3871-3877.
Boll, E.; Dheur, J.; Drobecq, H.; Melnyk, O. Access to Cyclic or Branched Peptides Using Bis(2-Sulfanylethyl)Amido Side-Chain Derivatives of Asp and Glu. Org. Lett. 2012, 14, 2222-2225.
Naruse, N.; Ohkawachi, K.; Inokuma, T.; Shigenaga, A.; Otaka, A. Resin-Bound Crypto-Thioester for Native Chemical Ligation. Org. Lett. 2018, 20, 2449-2453.
Nakahara, Y.; Matsuo, I.; Ito, Y.; Ubagai, R.; Hojo, H.; Nakahara, Y. High-Pressure-Promoted Fmoc-Aminoacylation of NEthylcysteine: Preparation of Key Devices for the Solid-Phase Synthesis of Peptide Thioesters. Tetrahedron Lett. 2010, 51, 407-410.
Asahina, Y.; Nabeshima, K.; Hojo, H. Peptidyl NAlkylcysteine as a Peptide Thioester Surrogate in the Native Chemical Ligation. Tetrahedron Lett. 2015, 56, 1370-1373.
Tsuda, S.; Mochizuki, M.; Sakamoto, K.; Denda, M.; Nishio, H.; Otaka, A.; Yoshiya, T. N-Sulfanylethylaminooxybutyramide (SEAoxy): A Crypto-Thioester Compatible with Fmoc Solid-Phase Peptide Synthesis. Org. Lett. 2016, 18, 5940-5943.
Rao, C.; Liu, C. F. Peptide Weinreb Amide Derivatives as Thioester Precursors for Native Chemical Ligation. Org. Biomol. Chem. 2017, 15, 2491-2496.
Reimer, U.; El Mokdad, N.; Schutkowski, M.; Fischer, G. Intramolecular Assistance of Cis/Trans Isomerization of the Histidine-Proline Moiety. Biochemistry 1997, 36, 13802-13808.
Szostak, R.; Aube, J.; Szostak, M. An Efficient Computational Model to Predict Protonation at the Amide Nitrogen and Reactivity Along the C-N Rotational Pathway. Chem. Commun. 2015, 51, 6395-6398.
Fersht, A. R. Acyl-Transfer Reactions of Amides and Esters with Alcohols and Thiols. Reference System for the Serine and Cysteine Proteinases. Nitrogen Protonation of Amides and Amide-Imidate Equilibriums. J. Am. Chem. Soc. 1971, 93, 3504-3515.
Kellogg, B. A.; Neverov, A. A.; Aman, A. M.; Brown, R. S. Catalysis of Acyl Transfer from Amides to Thiolate Nucleophiles: The Reaction of a Distorted Anilide with Thioglycolic Acid and Ethyl 2-Mercaptoacetate. J. Am. Chem. Soc. 1996, 118, 10829-10837.
Leliévre, D.; Terrier, V. P.; Delmas, A. F.; Aucagne, V. Native Chemical Ligation Strategy to Overcome Side Reactions During Fmoc-Based Synthesis of C-Terminal Cysteine-Containing Peptides. Org. Lett. 2016, 18, 920-923.
Terrier, V. P.; Delmas, A. F.; Aucagne, V. Efficient Synthesis of Cysteine-Rich Cyclic Peptides through Intramolecular Native Chemical Ligation of N-Hnb-Cys Peptide Crypto-Thioesters. Org. Biomol. Chem. 2017, 15, 316-319.
Jung, M. E.; Piizzi, G. Gem-Disubstituent Effect: Theoretical Basis and Synthetic Applications. Chem. Rev. 2005, 105, 1735-1766.
Raibaut, L.; Drobecq, H.; Melnyk, O. Selectively Activatable Latent Thiol and Selenolesters Simplify the Access to Cyclic or Branched Peptide Scaffolds. Org. Lett. 2015, 17, 3636-3639.
Botti, P.; Villain, M.; Manganiello, S.; Gaertner, H. Native Chemical Ligation through in Situ O to S Acyl Shift. Org. Lett. 2004, 6, 4861-4864.
Zheng, J. S.; Cui, H. K.; Fang, G. M.; Xi, W. X.; Liu, L. Chemical Protein Synthesis by Kinetically Controlled Ligation of Peptide O-Esters. ChemBioChem 2010, 11, 511-515.
Baumruck, A. C.; Tietze, D.; Steinacker, L. K.; Tietze, A. A. Chemical Synthesis of Membrane Proteins: A Model Study on the Influenza Virus B Proton Channel. Chem. Sci. 2018, 9, 2365-2375.
Zheng, J.-S.; Chang, H.-N.; Shi, J.; Liu, L. Chemical Synthesis of a Cyclotide via Intramolecular Cyclization of Peptide O-Esters. Sci. China: Chem. 2012, 55, 64-69.
Tofteng, A. P.; Jensen, K. J.; Hoeg-Jensen, T. Peptide Dithiodiethanol Esters for in Situ Generation of Thioesters for Use in Native Ligation. Tetrahedron Lett. 2007, 48, 2105-2107.
Warren, J. D.; Miller, J. S.; Keding, S. J.; Danishefsky, S. J. Toward Fully Synthetic Glycoproteins by Ultimately Convergent Routes: A Solution to a Long-Standing Problem. J. Am. Chem. Soc. 2004, 126, 6576-6578.
Chen, G.; Warren, J. D.; Chen, J.; Wu, B.; Wan, Q.; Danishefsky, S. J. Studies Related to the Relative Thermodynamic Stability of C-Terminal Peptidyl Esters of o-Hydroxy Thiophenol: Emergence of a Doable Strategy for Non-Cysteine Ligation Applicable to the Chemical Synthesis of Glycopeptides. J. Am. Chem. Soc. 2006, 128, 7460-7462.
George, E. A.; Novick, R. P.; Muir, T. W. Cyclic Peptide Inhibitors of Staphylococcal Virulence Prepared by Fmoc-Based Thiolactone Peptide Synthesis. J. Am. Chem. Soc. 2008, 130, 4914-4924.
Martin, R. B.; Hedrick, R. I. Intramolecular S-O and S-N Acetyl Transfer Reactions. J. Am. Chem. Soc. 1962, 84, 106-110.
Wang, C.; Guo, Q.-X. Theoretical Study on Formation of Thioesters via O-to-S Acyl Transfer. Sci. China: Chem. 2012, 55, 2075-2080.
Pavlic, A. A.; Lazier, W. A.; Signaigo, F. K. Synthesis of Some Vicinal Dithiols and their Derivatives. J. Org. Chem. 1949, 14, 59-64.
Miles, L. W. C.; Owen, L. N. 149. Dithiols. Part XII. The Alkaline Hydrolysis of Acetylated Hydroxy-Thiols: A New Reaction for the Formation of Cyclic Sulphides. J. Chem. Soc. 1952, 817-826.
Harding, J. S.; Owen, L. N. Dithiols. Part XIII. The Alkaline Hydrolysis of Acetylated Vicinal Hydroxy-Thiols. J. Chem. Soc. 1954, 1528-1536.
Kawa, H.; Ishikawa, N. Formation of C-S Bond by the Elimination of Perfluorocarboxylic Acid. Bull. Chem. Soc. Jpn. 1980, 53, 2097-2098.
Gates, Z. P.; Stephan, J. R.; Lee, D. J.; Kent, S. B. H. Rapid Formal Hydrolysis of Peptide-?Thioesters. Chem. Commun. 2013, 49, 786-788.
Tsuji, K.; Shigenaga, A.; Sumikawa, Y.; Tanegashima, K.; Sato, K.; Aihara, K.; Hara, T.; Otaka, A. Application of N-C-or C-NDirected Sequential Native Chemical Ligation to the Preparation of CXCL14 Analogs and their Biological Evaluation. Bioorg. Med. Chem. 2011, 19, 4014-4020.
Mazmanian, K.; Sargsyan, K.; Grauffel, C.; Dudev, T.; Lim, C. Preferred Hydrogen-Bonding Partners of Cysteine: Implications for Regulating Cys Functions. J. Phys. Chem. B 2016, 120, 10288-10296.
Bruice, T. C. Imidazole Catalysis. Vi. The Intramolecular Nucleophilic Catalysis of the Hydrolysis of an Acyl Thiol. The Hydrolysis of n-Propyl ?-(4-Imidazolyl)-Thiolbutyrate. J. Am. Chem. Soc. 1959, 81, 5444-5449.
Fife, T. H.; DeMark, B. R. General-Base-Catalyzed Intramolecular Aminolysis of Thiol Esters. Cyclization of S-n-Propyl o-(2-Imidazolyl)thiolbenzoate. Relationship of the Uncatalyzed and Base-Catalyzed Nucleophilic Reactions. J. Am. Chem. Soc. 1979, 101, 7379-7385.
Wenck, H.; Polster, J. Mechanistische Untersuchung zur Acyl-Ubertragung von Thioestern auf Amino-und Imidazolgruppen. Helv. Chim. Acta 1973, 56, 2036-2044.
Wang, Y.; Han, L.; Yuan, N.; Wang, H.; Li, H.; Liu, J.; Chen, H.; Zhang, Q.; Dong, S. Traceless ?-Mercaptan-Assisted Activation of Valinyl Benzimidazolinones in Peptide Ligations. Chem. Sci. 2018, 9, 1940-1946.
Chen, H.; Xiao, Y.; Yuan, N.; Weng, J.; Gao, P.; Breindel, L.; Shekhtman, A.; Zhang, Q. Coupling of Sterically Demanding Peptides by ?-Thiolactone-Mediated Native Chemical Ligation. Chem. Sci. 2018, 9, 1982-1988.
Pollock, S. B.; Kent, S. B. H. An Investigation into the Origin of the Dramatically Reduced Reactivity of Peptide-Prolyl-Thioesters in Native Chemical Ligation. Chem. Commun. 2011, 47, 2342-2344.
Newberry, R. W.; Orke, S. J.; Raines, R. T. n Interactions Are Competitive with Hydrogen Bonds. Org. Lett. 2016, 18, 3614-3617.
Bartlett, G. J.; Choudhary, A.; Raines, R. T.; Woolfson, D. N. n Interactions in Proteins. Nat. Chem. Biol. 2010, 6, 615-620.
Newberry, R. W.; Raines, R. T. The n Interaction. Acc. Chem. Res. 2017, 50, 1838-1846.
Hodges, J. A.; Raines, R. T. Energetics of an n Interaction That Impacts Protein Structure. Org. Lett. 2006, 8, 4695-4697.
Choudhary, A.; Fry, C. G.; Kamer, K. J.; Raines, R. T. An n? ? Interaction Reduces the Electrophilicity of the Acceptor Carbonyl Group. Chem. Commun. 2013, 49, 8166-8168.
Guzei, I. A.; Choudhary, A.; Raines, R. T. Pyramidalization of a Carbonyl C Atom in (2s)-N-(Selenoacetyl)Proline Methyl Ester. Acta Crystallogr., Sect. E: Struct. Rep. Online 2013, 69, o805-806.
Hinderaker, M. P.; Raines, R. T. An Electronic Effect on Protein Structure. Protein Sci. 2003, 12, 1188-1194.
Arnold, U.; Hinderaker, M. P.; Koditz, J.; Golbik, R.; Ulbrich-Hofmann, R.; Raines, R. T. Protein Prosthesis: A Nonnatural Residue Accelerates Folding and Increases Stability. J. Am. Chem. Soc. 2003, 125, 7500-7501.
Sasaki, K.; Crich, D. Cyclic Peptide Synthesis with Thioacids. Org. Lett. 2010, 12, 3254-3257.
Raibaut, L.; Seeberger, P.; Melnyk, O. Bis(2-Sulfanylethyl)-Amido Peptides Enable Native Chemical Ligation at Proline and Minimize Deletion Side-Product Formation. Org. Lett. 2013, 15, 5516-5519.
Sayers, J.; Karpati, P. M. T.; Mitchell, N. J.; Goldys, A. M.; Kwong, S. M.; Firth, N.; Chan, B.; Payne, R. J. Construction of Challenging Proline-Proline Junctions via Diselenide-Selenoester Ligation Chemistry. J. Am. Chem. Soc. 2018, 140, 13327-13334.
Gui, Y.; Qiu, L.; Li, Y.; Li, H.; Dong, S. Internal Activation of Peptidyl Prolyl Thioesters in Native Chemical Ligation. J. Am. Chem. Soc. 2016, 138, 4890-4899.
Ali Shah, M. I.; Xu, Z.-Y.; Liu, L.; Jiang, Y.-Y.; Shi, J. Mechanism for the Enhanced Reactivity of 4-Mercaptoprolyl Thioesters in Native Chemical Ligation. RSC Adv. 2016, 6, 68312-68321.
Camarero, J. A.; Muir, T. W. Native Chemical Ligation of Polypeptides. Curr. Protoc. Protein Sci. 1999, 18, 18. 14. 1.
Arnold, U.; Hinderaker, M. P.; Nilsson, B. L.; Huck, B. R.; Gellman, S. H.; Raines, R. T. Protein Prosthesis: A Semisynthetic Enzyme with a Beta-Peptide Reverse Turn. J. Am. Chem. Soc. 2002, 124, 8522-8523.
Gross, C. M.; Leliévre, D.; Woodward, C. K.; Barany, G. Preparation of Protected Peptidyl Thioester Intermediates for Native Chemical Ligation by N?-9-Fluorenylmethoxycarbonyl (Fmoc) Chemistry: Considerations of Side-Chain and Backbone Anchoring Strategies, and Compatible Protection for N-Terminal Cysteine. J. Pept. Res. 2005, 65, 395-410.
Bodanszky, M.; Martinez, J. Side Reactions in Peptide Synthesis. In The Peptides. Analysis, Synthesis, Biology; Gross, E., Meienhofer, J., Eds.; Academic Press: New York, 1983; Vol. 5, 111-216.
Dang, B.; Kubota, T.; Mandal, K.; Bezanilla, F.; Kent, S. B. H. Native Chemical Ligation at Asx-Cys, Glx-Cys: Chemical Synthesis and High-Resolution X-Ray Structure of ShK Toxin by Racemic Protein Crystallography. J. Am. Chem. Soc. 2013, 135, 11911-11919.
Raibaut, L.; Vicogne, J.; Leclercq, B.; Drobecq, H.; Desmet, R.; Melnyk, O. Total Synthesis of Biotinylated N Domain of Human Hepatocyte Growth Factor. Bioorg. Med. Chem. 2013, 21, 3486-3494.
Villain, M.; Gaertner, H.; Botti, P. Native Chemical Ligation with Aspartic and Glutamic Acids as C-Terminal Residues: Scope and Limitations. Eur. J. Org. Chem. 2003, 2003, 3267-3272.
Creech, G. S.; Paresi, C.; Li, Y. M.; Danishefsky, S. J. Chemical Synthesis of the ATAD2 Bromodomain. Proc. Aatl. Acad. Sci. U. S. A. 2014, 111, 2891-2896.
Jbara, M.; Eid, E.; Brik, A. Palladium Mediated Deallylation in Fully Aqueous Conditions for Native Chemical Ligation at Aspartic and Glutamic Acid Sites. Org. Biomol. Chem. 2018, 16, 4061-4064.
Mhidia, R.; Boll, E.; Fecourt, F.; Ermolenko, M.; Ollivier, N.; Sasaki, K.; Crich, D.; Delpech, B.; Melnyk, O. Exploration of an Imide Capture/N, N-Acyl Shift Sequence for Asparagine Native Peptide Bond Formation. Bioorg. Med. Chem. 2013, 21, 3479-3485.
Xu, C.; Xu, J.; Liu, H.; Li, X. Development of Aspartic Acid Ligation for Peptide Cyclization Derived from Serine/Threonine Ligation. Chin. Chem. Lett. 2018, 29, 1119-1122.
Dunkelmann, D. L.; Hirata, Y.; Totaro, K. A.; Cohen, D. T.; Zhang, C.; Gates, Z. P.; Pentelute, B. L. Amide-Forming Chemical Ligation via O-Acyl Hydroxamic Acids. Proc. Natl. Acad. Sci. U. S. A. 2018, 115, 3752-3757.
Goodman, M.; Stueben, K. C. Peptide Synthesis via Amino Acid Active Esters. II. Some Abnormal Reactions During Peptide Synthesis. J. Am. Chem. Soc. 1962, 84, 1279-1283.
Fischer, P. M. Diketopiperazines in Peptide and Combinatorial Chemistry. J. Pept. Sci. 2003, 9, 9-35.
Seenaiah, M.; Jbara, M.; Mali, S. M.; Brik, A. Convergent Versus Sequential Protein Synthesis: The Case of Ubiquitinated and Glycosylated H2B. Angew. Chem., Int. Ed. 2015, 54, 12374-12378.
Deng, F. K.; Zhang, L.; Wang, Y. T.; Schneewind, O.; Kent, S. B. H. Total Chemical Synthesis of the Enzyme Sortase A(?N59) with Full Catalytic Activity. Angew. Chem., Int. Ed. 2014, 53, 4662-4666.
Suzek, B. E.; Huang, H.; McGarvey, P.; Mazumder, R.; Wu, C. H. Uniref: Comprehensive and Non-Redundant Uniprot Reference Clusters. Bioinformatics 2007, 23, 1282-1288.
Miseta, A.; Csutora, P. Relationship between the Occurrence of Cysteine in Proteins and the Complexity of Organisms. Mol. Biol. Evol. 2000, 17, 1232-1239.
Carugo, O. Amino Acid Composition and Protein Dimension. Protein Sci. 2008, 17, 2187-2191.
Vizzavona, J.; Dick, F.; Vorherr, T. Synthesis and Application of an Auxiliary Group for Chemical Ligation at the X-Gly Site. Bioorg. Med. Chem. Lett. 2002, 12, 1963-1965.
Nakamura, K.; Sumida, M.; Kawakami, T.; Vorherr, T.; Aimoto, S. Generation of an S-Peptide via an N-S Acyl Shift Reaction in a TFA Solution. Bull. Chem. Soc. Jpn. 2006, 79, 1773-1780.
Nakamura, K.; Kanao, T.; Uesugi, T.; Hara, T.; Sato, T.; Kawakami, T.; Aimoto, S. Synthesis of Peptide Thioesters via an N-S Acyl Shift Reaction under Mild Acidic Conditions on an N-4, 5-Dimethoxy-2-Mercaptobenzyl Auxiliary Group. J. Pept. Sci. 2009, 15, 731-737.
Nadler, C.; Nadler, A.; Hansen, C.; Diederichsen, U. A Photocleavable Auxiliary for Extended Native Chemical Ligation. Eur. J. Org. Chem. 2015, 2015, 3095-3102.
Offer, J.; Dawson, P. E. N?-2-Mercaptobenzylamine-Assisted Chemical Ligation. Org. Lett. 2000, 2, 23-26.
Kawakami, T.; Akaji, K.; Aimoto, S. Peptide Bond Formation Mediated by 4, 5-Dimethoxy-2-Mercaptobenzylamine after Periodate Oxidation of the N-Terminal Serine Residue. Org. Lett. 2001, 3, 1403-1405.
Canne, L. E.; Bark, S. J.; Kent, S. B. H. Extending the Applicability of Native Chemical Ligation. J. Am. Chem. Soc. 1996, 118, 5891-5896.
Yang, R.; Bi, X.; Li, F.; Cao, Y.; Liu, C.-F. Native Chemical Ubiquitination Using a Genetically Incorporated Azidonorleucine. Chem. Commun. 2014, 50, 7971-7974.
Xu, L.; Huang, J.-F.; Chen, C.-C.; Qu, Q.; Shi, J.; Pan, M.; Li, Y.-M. Chemical Synthesis of Natural Polyubiquitin Chains through Auxiliary-Mediated Ligation of an Expressed Ubiquitin Isomer. Org. Lett. 2018, 20, 329-332.
Loibl, S. F.; Harpaz, Z.; Seitz, O. A Type of Auxiliary for Native Chemical Peptide Ligation Beyond Cysteine and Glycine Junctions. Angew. Chem., Int. Ed. 2015, 54, 15055-15059.
Marinzi, C.; Bark, S. J.; Offer, J.; Dawson, P. E. A New Scaffold for Amide Ligation. Bioorg. Med. Chem. 2001, 9, 2323-2328.
Weller, C. E.; Dhall, A.; Ding, F.; Linares, E.; Whedon, S. D.; Senger, N. A.; Tyson, E. L.; Bagert, J. D.; Li, X.; Augusto, O.; Chatterjee, C. Aromatic Thiol-Mediated Cleavage of N-O Bonds Enables Chemical Ubiquitylation of Folded Proteins. Nat. Commun. 2016, 7, No. 12979.
Botti, P.; Carrasco, M. R.; Kent, S. B. H. Native Chemical Ligation Using Removable N?-(1-Phenyl-2-Mercaptoethyl) Auxiliaries. Tetrahedron Lett. 2001, 42, 1831-1833.
Macmillan, D.; Anderson, D. W. Rapid Synthesis of Acyl Transfer Auxiliaries for Cysteine-Free Native Glycopeptide Ligation. Org. Lett. 2004, 6, 4659-4662.
Harpaz, Z.; Loibl, S.; Seitz, O. Native Chemical Ligation at a Base-Labile 4-Mercaptobutyrate N(?)-Auxiliary. Bioorg. Med. Chem. Lett. 2016, 26, 1434-1437.
Haase, C.; Rohde, H.; Seitz, O. Native Chemical Ligation at Valine. Angew. Chem., Int. Ed. 2008, 47, 6807-6810.
Sayers, J.; Thompson, R. E.; Perry, K. J.; Malins, L. R.; Payne, R. J. Thiazolidine-Protected ?-Thiol Asparagine: Applications in One-Pot Ligation-Desulfurization Chemistry. Org. Lett. 2015, 17, 4902-4905.
Thompson, R. E.; Chan, B.; Radom, L.; Jolliffe, K. A.; Payne, R. J. Chemoselective Peptide Ligation-Desulfurization at Aspartate. Angew. Chem., Int. Ed. 2013, 52, 9723-9727.
Crich, D.; Banerjee, A. Native Chemical Ligation at Phenylalanine. J. Am. Chem. Soc. 2007, 129, 10064-10065.
Malins, L. R.; Giltrap, A. M.; Dowman, L. J.; Payne, R. J. Synthesis of ?-Thiol Phenylalanine for Applications in One-Pot Ligation-Desulfurization Chemistry. Org. Lett. 2015, 17, 2070-2073.
Malins, L. R.; Cergol, K. M.; Payne, R. J. Peptide Ligation-Desulfurization Chemistry at Arginine. ChemBioChem 2013, 14, 559-563.
Chen, J.; Wan, Q.; Yuan, Y.; Zhu, J.; Danishefsky, S. J. Native Chemical Ligation at Valine: A Contribution to Peptide and Glycopeptide Synthesis. Angew. Chem., Int. Ed. 2008, 47, 8521-8524.
Tan, Z.; Shang, S.; Danishefsky, S. J. Insights into the Finer Issues of Native Chemical Ligation: An Approach to Cascade Ligations. Angew. Chem., Int. Ed. 2010, 49, 9500-9503.
Shang, S.; Tan, Z.; Danishefsky, S. J. Application of the Logic of Cysteine-Free Native Chemical Ligation to the Synthesis of Human Parathyroid Hormone (hPTH). Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 5986-5989.
Guan, X.; Drake, M. R.; Tan, Z. Total Synthesis of Human Galanin-Like Peptide through an Aspartic Acid Ligation. Org. Lett. 2013, 15, 6128-6131.
Matsugi, M.; Kita, Y. 2, 2?-Azobis(2-methylpropanimidamide) Dihydrochloride (V-50). In e-EROS; John Wiley & Sons, Ltd, 2007; DOI: 10. 1002/047084289X. rn00727
Xin, B. T.; van Tol, B. D. M.; Ovaa, H.; Geurink, P. P. Native Chemical Ligation at Methionine Bioisostere Norleucine Allows for N-Terminal Chemical Protein Ligation. Org. Biomol. Chem. 2018, 16, 6306-6315.
Merkx, R.; de Bruin, G.; Kruithof, A.; van den Bergh, T.; Snip, E.; Lutz, M.; El Oualid, F.; Ovaa, H. Scalable Synthesis of ?-Thiolysine Starting from Lysine and a Side by Side Comparison with ?-Thiolysine in Non-Enzymatic Ubiquitination. Chem. Sci. 2013, 4, 4494-4498.
Pasunooti, K. K.; Yang, R.; Banerjee, B.; Yap, T.; Liu, C.-F. 5-Methylisoxazole-3-Carboxamide-Directed Palladium-Catalyzed ?-C-(sp3)-H Acetoxylation and Application to the Synthesis of ?-Mercapto Amino Acids for Native Chemical Ligation. Org. Lett. 2016, 18, 2696-2699.
Cergol, K. M.; Thompson, R. E.; Malins, L. R.; Turner, P.; Payne, R. J. One-Pot Peptide Ligation-Desulfurization at Glutamate. Org. Lett. 2014, 16, 290-293.
Siman, P.; Karthikeyan, S. V.; Brik, A. Native Chemical Ligation at Glutamine. Org. Lett. 2012, 14, 1520-1523.
Chen, J.; Wang, P.; Zhu, J.; Wan, Q.; Danishefsky, S. J. A Program for Ligation at Threonine Sites: Application to the Controlled Total Synthesis of Glycopeptides. Tetrahedron 2010, 66, 2277-2283.
Shang, S.; Tan, Z.; Dong, S.; Danishefsky, S. J. An Advance in Proline Ligation. J. Am. Chem. Soc. 2011, 133, 10784-10786.
Ding, H.; Shigenaga, A.; Sato, K.; Morishita, K.; Otaka, A. Dual Kinetically Controlled Native Chemical Ligation Using a Combination of Sulfanylproline and Sulfanylethylanilide Peptide. Org. Lett. 2011, 13, 5588-5591.
Yang, R.; Pasunooti, K. K.; Li, F.; Liu, X.-W.; Liu, C.-F. Synthesis of K48-Linked Diubiquitin Using Dual Native Chemical Ligation at Lysine. Chem. Commun. 2010, 46, 7199-7201.
Yang, R.; Pasunooti, K. K.; Li, F.; Liu, X. W.; Liu, C. F. Dual Native Chemical Ligation at Lysine. J. Am. Chem. Soc. 2009, 131, 13592-13593.
Tam, J. P.; Yu, Q. Methionine Ligation Strategy in the Biomimetic Synthesis of Parathyroid Hormones. Biopolymers 1998, 46, 319-327.
Pachamuthu, K.; Schmidt, R. R. Synthesis of Methionine Containing Peptides Related to Native Chemical Ligation. Synlett 2003, 0659-0662.
Malins, L. R.; Cergol, K. M.; Payne, R. J. Chemoselective Sulfenylation and Peptide Ligation at Tryptophan. Chem. Sci. 2014, 5, 260-266.
Malins, L. R.; Payne, R. J. Synthesis and Utility of Beta-Selenol-Phenylalanine for Native Chemical Ligation-Deselenization Chemistry. Org. Lett. 2012, 14, 3142-3145.
Wang, X.; Sanchez, J.; Stone, M. J.; Payne, R. J. Sulfation of the Human Cytomegalovirus Protein UL22A Enhances Binding to the Chemokine RANTES. Angew. Chem., Int. Ed. 2017, 56, 8490-8494.
Mitchell, N. J.; Sayers, J.; Kulkarni, S. S.; Clayton, D.; Goldys, A. M.; Ripoll-Rozada, J.; Barbosa Pereira, P. J.; Chan, B.; Radom, L.; Payne, R. J. Accelerated Protein Synthesis via One-Pot Ligation-Deselenization Chemistry. Chem. 2017, 2, 703-715.
Townsend, S. D.; Tan, Z.; Dong, S.; Shang, S.; Brailsford, J. A.; Danishefsky, S. J. Advances in Proline Ligation. J. Am. Chem. Soc. 2012, 134, 3912-3916.
Turner, R. A.; Pierce, J. G.; Du Vigneaud, V. The Desulfurization of Oxytocin. J. Biol. Chem. 1951, 193, 359-361.
He, S.; Bauman, D.; Davis, J. S.; Loyola, A.; Nishioka, K.; Gronlund, J. L.; Reinberg, D.; Meng, F.; Kelleher, N.; McCafferty, D. G. Facile Synthesis of Site-Specifically Acetylated and Methylated Histone Proteins: Reagents for Evaluation of the Histone Code Hypothesis. Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 12033-12038.
Bentrude, W. G. Phosphoranyl Radicals-their Structure, Formation, and Reactions. Acc. Chem. Res. 1982, 15, 117-125.
Bentrude, W. G.; Hansen, E. R.; Khan, W. A.; Min, T. B.; Rogers, P. E. Free-Radical Chemistry of Organophosphorus Compounds. III. ? vs. ? Scission in Reactions of Alkoxy and Thiyl Radicals with Trivalent Organophosphorus Derivatives. J. Am. Chem. Soc. 1973, 95, 2286-2293.
Tian, Y.; Wang, L.; Shi, J.; Yu, H.-z. Desulfurization Mechanism of Cysteine in Synthesis of Polypeptides. Chin. J. Chem. Phys. 2015, 28, 269-276.
Jin, K.; Li, T.; Chow, H. Y.; Liu, H.; Li, X. P-B Desulfurization: An Enabling Method for Protein Chemical Synthesis and Site-Specific Deuteration. Angew. Chem., Int. Ed. 2017, 56, 14607-14611.
Geurink, P. P.; El Oualid, F.; Jonker, A.; Hameed, D. S.; Ovaa, H. A General Chemical Ligation Approach Towards Isopeptide-Linked Ubiquitin and Ubiquitin-Like Assay Reagents. ChemBioChem 2012, 13, 293-297.
Cross, R. J.; Millington, D. Selenium Abstraction from Diethyl Diselenide by Tertiary Phosphines. J. Chem. Soc., Chem. Commun. 1975, 455-456.
Chu, J. Y. C.; Marsh, D. G. Photochemistry of Organochalcogen Compounds. 2. Photochemical Deselenation of Benzyl Diselenide by Triphenylphosphine. J. Org. Chem. 1976, 41, 3204-3205.
McMillen, D. F.; Golden, D. M. Hydrocarbon Bond Dissociation Energies. Annu. Rev. Phys. Chem. 1982, 33, 493-532.
Rauk, A.; Yu, D.; Armstrong, D. A. Oxidative Damage to and by Cysteine in Proteins: An ab Initio Study of the Radical Structures, C-H, S-H, and C-C Bond Dissociation Energies, and Transition Structures for H Abstraction by Thiyl Radicals. J. Am. Chem. Soc. 1998, 120, 8848-8855.
Pearson, J. K.; Ban, F.; Boyd, R. J. An Evaluation of Various Computational Methods for the Treatment of Organoselenium Compounds. J. Phys. Chem. A 2005, 109, 10373-10379.
Kaur, D.; Sharma, P.; Bharatam, P. V.; Kaur, M. Understanding Selenocysteine through Conformational Analysis, Proton Affinities, Acidities and Bond Dissociation Energies. Int. J. Quantum Chem. 2008, 108, 983-991.
Nauser, T.; Dockheer, S.; Kissner, R.; Koppenol, W. H. Catalysis of Electron Transfer by Selenocysteine. Biochemistry 2006, 45, 6038-6043.
Bingham, J. P.; Chun, J. B.; Ruzicka, M. R.; Li, Q. X.; Tan, Z. Y.; Kaulin, Y. A.; Englebretsen, D. R.; Moczydlowski, E. G. Synthesis of an Iberiotoxin Derivative by Chemical Ligation: A Method for Improved Yields of Cysteine-Rich Scorpion Toxin Peptides. Peptides 2009, 30, 1049-1057.
Tsuda, S.; Mochizuki, M.; Ishiba, H.; Yoshizawa-Kumagaye, K.; Nishio, H.; Oishi, S.; Yoshiya, T. Easy-to-Attach/Detach Solubilizing-Tag-Aided Chemical Synthesis of an Aggregative Capsid Protein. Angew. Chem., Int. Ed. 2018, 57, 2105-2109.
Lim, I. S.; Lim, J. S.; Lee, Y. S.; Kim, S. K. Experimental and Theoretical Study of the Photodissociation Reaction of Thiophenol at 243 nm: Intramolecular Orbital Alignment of the Phenylthiyl Radical. J. Chem. Phys. 2007, 126, 034306.
Borges dos Santos, R. M.; Muralha, V. S. F.; Correia, C. F.; Guedes, R. C.; Costa Cabral, B. J.; Martinho Simóes, J. A. S-H Bond Dissociation Enthalpies in Thiophenols: A Time-Resolved Photoacoustic Calorimetry and Quantum Chemistry Study. J. Phys. Chem. A 2002, 106, 9883-9889.
Shimko, J. C.; Howard, C. J.; Poirier, M. G.; Ottesen, J. J. Preparing Semisynthetic and Fully Synthetic Histones H3 and H4 to Modify the Nucleosome Core. Methods Mol. Biol. 2013, 981, 177-192.
Reimann, O.; Smet-Nocca, C.; Hackenberger, C. P. R. Traceless Purification and Desulfurization of Tau Protein Ligation Products. Angew. Chem., Int. Ed. 2015, 54, 306-310.
Moyal, T.; Hemantha, H. P.; Siman, P.; Refua, M.; Brik, A. Highly Efficient One-Pot Ligation and Desulfurization. Chem. Sci. 2013, 4, 2496-2501.
Malins, L. R.; Payne, R. J. Recent Extensions to Native Chemical Ligation for the Chemical Synthesis of Peptides and Proteins. Curr. Opin. Chem. Biol. 2014, 22, 70-78.
Premdjee, B.; Payne, R. J. Synthesis of Proteins by Native Chemical Ligation-Desulfurization Strategies. In Chemical Ligation: Tools for Biomolecule Synthesis and Modification; D'Andrea, L. D., Romanelli, A., Eds.; John Wiley & Sons: New York, 2017, 161-218.
Chen, S. Y.; Cressman, S.; Mao, F.; Shao, H.; Low, D. W.; Beilan, H. S.; Cagle, E. N.; Carnevali, M.; Gueriguian, V.; Keogh, P. J.; et al. Synthetic Erythropoietic Proteins: Tuning Biological Performance by Site-Specific Polymer Attachment. Chem. Biol. 2005, 12, 371-383.
Macmillan, D.; Bertozzi, C. R. Modular Assembly of Glycoproteins: Towards the Synthesis of GlyCAM-1 by Using Expressed Protein Ligation. Angew. Chem., Int. Ed. 2004, 43, 1355-1359.
Torbeev, V. Y.; Kent, S. B. H. Ionization State of the Catalytic Dyad Asp25/25' in the HIV-1 Protease: NMR Studies of Site-Specifically 13C Labelled HIV-1 Protease Prepared by Total Chemical Synthesis. Org. Biomol. Chem. 2012, 10, 5887-5891.
Bang, D.; Kent, S. B. H. His6 Tag-Assisted Chemical Protein Synthesis. Proc. Natl. Acad. Sci. U. S. A. 2005, 102, 5014-5019.
Gordon, W. R.; Bang, D.; Hoff, W. D.; Kent, S. B. H. Total Chemical Synthesis of Fully Functional Photoactive Yellow Protein. Bioorg. Med. Chem. 2013, 21, 3436-3442.
Johnson, E. C.; Malito, E.; Shen, Y.; Pentelute, B.; Rich, D.; Florian, J.; Tang, W. J.; Kent, S. B. H. Insights from Atomic-Resolution X-Ray Structures of Chemically Synthesized HIV-1 Protease in Complex with Inhibitors. J. Mol. Biol. 2007, 373, 573-586.
Allahverdi, A.; Yang, R.; Korolev, N.; Fan, Y.; Davey, C. A.; Liu, C. F.; Nordenskiold, L. The Effects of Histone H4 Tail Acetylations on Cation-Induced Chromatin Folding and Self-Association. Nucleic Acids Res. 2011, 39, 1680-1691.
Sato, K.; Shigenaga, A.; Kitakaze, K.; Sakamoto, K.; Tsuji, D.; Itoh, K.; Otaka, A. Chemical Synthesis of Biologically Active Monoglycosylated GM2-Activator Protein Analogue Using NSulfanylethylanilide Peptide. Angew. Chem., Int. Ed. 2013, 52, 7855-7859.
Murase, T.; Kajihara, Y. Synthesis of the Glycosylated Polypeptide Chain of an Inducible Costimulator on T-Cells. Carbohydr. Res. 2010, 345, 1324-1330.
Okamoto, R.; Souma, S.; Kajihara, Y. Efficient Substitution Reaction from Cysteine to the Serine Residue of Glycosylated Polypeptide: Repetitive Peptide Segment Ligation Strategy and the Synthesis of Glycosylated Tetracontapeptide Having Acid Labile Sialyl-Tn Antigens. J. Org. Chem. 2009, 74, 2494-2501.
Tanaka, T.; Wagner, A. M.; Warner, J. B.; Wang, Y. J.; Petersson, E. J. Expressed Protein Ligation at Methionine: NTerminal Attachment of Homocysteine, Ligation, and Masking. Angew. Chem., Int. Ed. 2013, 52, 6210-6213.
Dardashti, R. N.; Metanis, N. Revisiting Ligation at Selenomethionine: Insights into Native Chemical Ligation at Selenocysteine and Homoselenocysteine. Bioorg. Med. Chem. 2017, 25, 4983-4989.
Haj-Yahya, N.; Hemantha, H. P.; Meledin, R.; Bondalapati, S.; Seenaiah, M.; Brik, A. Dehydroalanine-Based Diubiquitin Activity Probes. Org. Lett. 2014, 16, 540-543.
Chalker, J. M.; Lercher, L.; Rose, N. R.; Schofield, C. J.; Davis, B. G. Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications. Angew. Chem., Int. Ed. 2012, 51, 1835-1839.
Mulder, M. P. C.; Merkx, R.; Witting, K. F.; Hameed, D. S.; El Atmioui, D.; Lelieveld, L.; Liebelt, F.; Neefjes, J.; Berlin, I.; Vertegaal, A. C. O.; et al. Total Chemical Synthesis of SUMO and SUMO-Based Probes for Profiling the Activity of SUMO-Specific Proteases. Angew. Chem., Int. Ed. 2018, 57, 8958-8962.
Chalker, J. M.; Bernardes, G. J.; Lin, Y. A.; Davis, B. G. Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology. Chem.-Asian J. 2009, 4, 630-640.
Siman, P.; Brik, A. Chemical and Semisynthesis of Posttranslationally Modified Proteins. Org. Biomol. Chem. 2012, 10, 5684-5697.
Howard, C. J.; Yu, R. R.; Gardner, M. L.; Shimko, J. C.; Ottesen, J. J. Chemical and Biological Tools for the Preparation of Modified Histone Proteins. Top. Curr. Chem. 2015, 363, 193-226.
Katritzky, A. R.; Abo-Dya, N. E.; Tala, S. R.; Abdel-Samii, Z. K. The Chemical Ligation of Selectively S-Acylated Cysteine Peptides to Form Native Peptides via 5-, 11-and 14-Membered Cyclic Transition States. Org. Biomol. Chem. 2010, 8, 2316-2319.
Katritzky, A. R.; Tala, S. R.; Abo-Dya, N. E.; Ibrahim, T. S.; El-Feky, S. A.; Gyanda, K.; Pandya, K. M. Chemical Ligation of SAcylated Cysteine Peptides to Form Native Peptides via 5-, 11-, and 14-Membered Cyclic Transition States. J. Org. Chem. 2011, 76, 85-96.
Hansen, F. K.; Ha, K.; Todadze, E.; Lillicotch, A.; Frey, A.; Katritzky, A. R. Microwave-Assisted Chemical Ligation of S-Acyl Peptides Containing Non-Terminal Cysteine Residues. Org. Biomol. Chem. 2011, 9, 7162-7167.
Ha, K.; Chahar, M.; Monbaliu, J. C.; Todadze, E.; Hansen, F. K.; Oliferenko, A. A.; Ocampo, C. E.; Leino, D.; Lillicotch, A.; Stevens, C. V.; et al. Long-Range Intramolecular S-> N Acyl Migration: A Study of the Formation of Native Peptide Analogues via 13-, 15-, and 16-Membered Cyclic Transition States. J. Org. Chem. 2012, 77, 2637-2648.
Panda, S. S.; El-Nachef, C.; Bajaj, K.; Al-Youbi, A. O.; Oliferenko, A.; Katritzky, A. R. Study of Chemical Ligation via 17-, 18-and 19-Membered Cyclic Transition States. Chem. Biol. Drug Des. 2012, 80, 821-827.
Haase, C.; Seitz, O. Internal Cysteine Accelerates Thioester-Based Peptide Ligation. Eur. J. Org. Chem. 2009, 2009, 2096-2101.
Oliferenko, A. A.; Katritzky, A. R. Alternating Chemical Ligation Reactivity of S-Acyl Peptides Explained with Theory and Computations. Org. Biomol. Chem. 2011, 9, 4756-4759.
Bol'shakov, O.; Kovacs, J.; Chahar, M.; Ha, K.; Khelashvili, L.; Katritzky, A. R. S-to N-Acyl Transfer in S-Acylcysteine Isopeptides via 9-, 10-, 12-, and 13-Membered Cyclic Transition States. J. Pept. Sci. 2012, 18, 704-709.
Monbaliu, J.-C. M.; Dive, G.; Stevens, C. V.; Katritzky, A. R. Governing Parameters of Long-Range Intramolecular S-to-N Acyl Transfers within (S)-Acyl Isopeptides. J. Chem. Theory Comput. 2013, 9, 927-934.
Monbaliu, J. C.; Katritzky, A. R. Recent Trends in Cys-and Ser/Thr-Based Synthetic Strategies for the Elaboration of Peptide Constructs. Chem. Commun. 2012, 48, 11601-11622.
Panda, S. S.; Hall, C. D.; Oliferenko, A. A.; Katritzky, A. R. Traceless Chemical Ligation from S-, O-, and N-Acyl Isopeptides. Acc. Chem. Res. 2014, 47, 1076-1087.
Galli, C.; Illuminati, G.; Mandolini, L.; Tamborra, P. Ring-Closure Reactions. 7. Kinetics and Activation Parameters of Lactone Formation in the Range of 3-to 23-Membered Rings. J. Am. Chem. Soc. 1977, 99, 2591-2597.
Galli, C.; Illuminati, G.; Mandolini, L. Ring-Closure Reactions. 14. Kinetics of Macrocyclization by the Intramolecular Acylation of Thiophene and Benzothiophene Compounds. J. Org. Chem. 1980, 45, 311-315.
Cort, A. D.; Illuminati, G.; Mandolini, L.; Masci, B. Ring-Closure Reactions. Part 15. Solvent Effects on Cyclic Aralkyl Ether Formation by Intramolecular Williamson Synthesis. J. Chem. Soc., Perkin Trans. 2 1980, 2, 1774-1777.
Illuminati, G.; Mandolini, L. Ring Closure Reactions of Bifunctional Chain Molecules. Acc. Chem. Res. 1981, 14, 95-102.
Lightstone, F. C.; Bruice, T. C. Enthalpy and Entropy in Ring Closure Reactions. Bioorg. Chem. 1998, 26, 193-199.
Galli, C.; Mandolini, L. The Role of Ring Strain on the Ease of Ring Closure of Bifunctional Chain Molecules. Eur. J. Org. Chem. 2000, 2000, 3117-3125.
Menger, F. M. On the Source of Intramolecular and Enzymatic Reactivity. Acc. Chem. Res. 1985, 18, 128-134.
Houk, K. N.; Tucker, J. A.; Dorigo, A. E. Quantitative Modeling of Proximity Effects on Organic Reactivity. Acc. Chem. Res. 1990, 23, 107-113.
Lightstone, F. C.; Bruice, T. C. Separation of Ground State and Transition State Effects in Intramolecular and Enzymatic Reactions. 2. A Theoretical Study of the Formation of Transition States in Cyclic Anhydride Formation. J. Am. Chem. Soc. 1997, 119, 9103-9113.
Bruice, T. C.; Lightstone, F. C. Ground State and Transition State Contributions to the Rates of Intramolecular and Enzymatic Reactions. Acc. Chem. Res. 1999, 32, 127-136.
Martí-Centelles, V.; Pandey, M. D.; Burguete, M. I.; Luis, S. V. Macrocyclization Reactions: The Importance of Conformational, Configurational, and Template-Induced Preorganization. Chem. Rev. 2015, 115, 8736-8834.
Bruice, T. C. Some Pertinent Aspects of Mechanism as Determined with Small Molecules. Annu. Rev. Biochem. 1976, 45, 331-373.
Galli, C.; Illuminati, G.; Mandolini, L. Ring-Closure Reactions. I. Kinetics of Lactone Formation in the Range of Seven-to Twelve-Membered Rings. J. Am. Chem. Soc. 1973, 95, 8374-8379.
Galli, C.; Giovannelli, G.; Illuminati, G.; Mandolini, L. Ring-Closure Reactions. 12. Gem-Dimethyl Effect in Some Medium and Large Rings. J. Org. Chem. 1979, 44, 1258-1261.
Payne, R. J.; Ficht, S.; Tang, S.; Brik, A.; Yang, Y. Y.; Case, D. A.; Wong, C. H. Extended Sugar-Assisted Glycopeptide Ligations: Development, Scope, and Applications. J. Am. Chem. Soc. 2007, 129, 13527-13536.
Lutsky, M.-Y.; Nepomniaschiy, N.; Brik, A. Peptide Ligation via Side-Chain Auxiliary. Chem. Commun. 2008, 1229-1231.
Ajish Kumar, K. S.; Harpaz, Z.; Haj-Yahya, M.; Brik, A. Side-Chain Assisted Ligation in Protein Synthesis. Bioorg. Med. Chem. Lett. 2009, 19, 3870-3874.
Brik, A.; Yang, Y. Y.; Ficht, S.; Wong, C. H. Sugar-Assisted Glycopeptide Ligation. J. Am. Chem. Soc. 2006, 128, 5626-5627.
Ficht, S.; Payne, R. J.; Brik, A.; Wong, C. H. Second-Generation Sugar-Assisted Ligation: A Method for the Synthesis of Cysteine-Containing Glycopeptides. Angew. Chem., Int. Ed. 2007, 46, 5975-5979.
Bennett, C. S.; Dean, S. M.; Payne, R. J.; Ficht, S.; Brik, A.; Wong, C. H. Sugar-Assisted Glycopeptide Ligation with Complex Oligosaccharides: Scope and Limitations. J. Am. Chem. Soc. 2008, 130, 11945-11952.
Hojo, H.; Ozawa, C.; Katayama, H.; Ueki, A.; Nakahara, Y.; Nakahara, Y. The Mercaptomethyl Group Facilitates an Efficient One-Pot Ligation at Xaa-Ser/Thr for (Glyco)Peptide Synthesis. Angew. Chem., Int. Ed. 2010, 49, 5318-5321.
O'Conner, C. J.; Wallace, R. G. A Phosphate-Catalysed Acyl Transfer Reaction. Hydrolysis of 4-Nitrophenyl Acetate in Phosphate Buffers. Aust. J. Chem. 1984, 37, 2559-2569.
El Seoud, O. A.; Ruasse, M.-F.; Rodrigues, W. A. Kinetics and Mechanism of Phosphate-Catalyzed Hydrolysis of Benzoate Esters: Comparison with Nucleophilic Catalysis by Imidazole and o-Iodosobenzoate. J. Chem. Soc., Perkin Trans. 2002, 2, 1053-1058.
Gill, M. S.; Neverov, A. A.; Brown, R. S. Dissection of Nucleophilic and General Base Roles for the Reaction of Phosphate with p-Nitrophenyl Thiolacetate, p-Nitrophenyl Thiolformate, and Phenyl Thiolacetate. J. Org. Chem. 1997, 62, 7351-7357.
Di Sabato, G.; Jencks, W. P. Mechanism and Catalysis of Reactions of Acyl Phosphates. II. Hydrolysis. J. Am. Chem. Soc. 1961, 83, 4400-4405.
Di Sabato, G.; Jencks, W. P. Mechanism and Catalysis of Reactions of Acyl Phosphates. I. Nucleophilic Reactions. J. Am. Chem. Soc. 1961, 83, 4393-4400.
Liu, Z.; Beaufils, D.; Rossi, J. C.; Pascal, R. Evolutionary Importance of the Intramolecular Pathways of Hydrolysis of Phosphate Ester Mixed Anhydrides with Amino Acids and Peptides. Sci. Rep. 2015, 4, 7440.
De Jersey, J.; Willadsen, P.; Zerner, B. Oxazolinone Intermediates in the Hydrolysis of Activated N-Acylamino Acid Esters. The Relevance of Oxazolinones to the Mechanism of Action of Serine Proteinases. Biochemistry 1969, 8, 1959-1967.
Snella, B.; Diemer, V.; Drobecq, H.; Agouridas, V.; Melnyk, O. Native Chemical Ligation at Serine Revisited. Org. Lett. 2018, 20, 7616-7619.
Bello, C.; Wang, S.; Meng, L.; Moremen, K. W.; Becker, C. F. W. A Pegylated Photocleavable Auxiliary Mediates the Sequential Enzymatic Glycosylation and Native Chemical Ligation of Peptides. Angew. Chem., Int. Ed. 2015, 54, 7711-7715.
Maity, S. K.; Mann, G.; Jbara, M.; Laps, S.; Kamnesky, G.; Brik, A. Palladium-Assisted Removal of a Solubilizing Tag from a Cys Side Chain to Facilitate Peptide and Protein Synthesis. Org. Lett. 2016, 18, 3026-3029.
Jacobsen, M. T.; Petersen, M. E.; Ye, X.; Galibert, M.; Lorimer, G. H.; Aucagne, V.; Kay, M. S. A Helping Hand to Overcome Solubility Challenges in Chemical Protein Synthesis. J. Am. Chem. Soc. 2016, 138, 11775-11782.
Zheng, J.-S.; Yu, M.; Qi, Y.-K.; Tang, S.; Shen, F.; Wang, Z.-P.; Xiao, L.; Zhang, L.; Tian, C.-L.; Liu, L. Expedient Total Synthesis of Small to Medium-Sized Membrane Proteins via Fmoc Chemistry. J. Am. Chem. Soc. 2014, 136, 3695-3704.
Zheng, J.-S.; He, Y.; Zuo, C.; Cai, X.-Y.; Tang, S.; Wang, Z. A.; Zhang, L.-H.; Tian, C.-L.; Liu, L. Robust Chemical Synthesis of Membrane Proteins through a General Method of Removable Backbone Modification. J. Am. Chem. Soc. 2016, 138, 3553-3561.
Yang, S.-H.; Wojnar, J. M.; Harris, P. W. R.; DeVries, A. L.; Evans, C. W.; Brimble, M. A. Chemical Synthesis of a Masked Analogue of the Fish Antifreeze Potentiating Protein (AFPP). Org. Biomol. Chem. 2013, 11, 4935-4942.
Li, J.-B.; Tang, S.; Zheng, J.-S.; Tian, C.-L.; Liu, L. Removable Backbone Modification Method for the Chemical Synthesis of Membrane Proteins. Acc. Chem. Res. 2017, 50, 1143-1153.
Palmer, D. C. Guanidine. In e-EROS; John Wiley & Sons, Ltd, 2001; DOI: 10. 1002/047084289X. rg013.
Schug, K. A.; Lindner, W. Noncovalent Binding between Guanidinium and Anionic Groups: Focus on Biological-and Synthetic-Based Arginine/Guanidinium Interactions with Phosph-[on]ate and Sulf[on]ate Residues. Chem. Rev. 2005, 105, 67-114.
O'Brien, E. P.; Dima, R. I.; Brooks, B.; Thirumalai, D. Interactions between Hydrophobic and Ionic Solutes in Aqueous Guanidinium Chloride and Urea Solutions: Lessons for Protein Denaturation Mechanism. J. Am. Chem. Soc. 2007, 129, 7346-7353.
Shao, Q.; Fan, Y.; Yang, L.; Gao, Y. Q. Counterion Effects on the Denaturing Activity of Guanidinium Cation to Protein. J. Chem. Theory Comput. 2012, 8, 4364-4373.
Garcia-Mira, M. M.; Sanchez-Ruiz, J. M. pH Corrections and Protein Ionization in Water/Guanidinium Chloride. Biophys. J. 2001, 81, 3489-3502.
Kwon, B.; Tietze, D.; White, P. B.; Liao, S. Y.; Hong, M. Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain. Protein Sci. 2015, 24, 1087-1099.
Chu, N. K.; Becker, C. F. Semisynthesis of Membrane-Attached Prion Proteins. Methods Enzymol. 2009, 462, 177-193.
Greene, R. F., Jr.; Pace, C. N. Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, Alpha-Chymotrypsin, and Beta-Lactoglobulin. J. Biol. Chem. 1974, 249, 5388-5393.
Dirnhuber, P.; Schutz, F. The Isomeric Transformation of Urea into Ammonium Cyanate in Aqueous Solutions. Biochem. J. 1948, 42, 628-632.
Stark, G. R. On the Reversible Reaction of Cyanate with Sulfhydryl Groups and the Determination of NH2-Terminal Cysteine and Cystine in Proteins. J. Biol. Chem. 1964, 239, 1411-1414.
Bianchi, E.; Ingenito, R.; Simon, R. J.; Pessi, A. Engineering and Chemical Synthesis of a Transmembrane Protein: The HCV Protease Cofactor Protein NS4A. J. Am. Chem. Soc. 1999, 121, 7698-7699.
Hunter, C. L.; Kochendoerfer, G. G. Native Chemical Ligation of Hydrophobic Peptides in Lipid Bilayer Systems. Bioconjugate Chem. 2004, 15, 437-440.
Noller, C. R.; Rockwell, W. C. The Preparation of Some Higher Alkylglucosides. J. Am. Chem. Soc. 1938, 60, 2076-2077.
Baron, C.; Thompson, T. E. Solubilization of Bacterial Membrane Proteins Using Alkyl Glucosides and Dioctanoyl Phosphatidylcholine. Biochim. Biophys. Acta, Biomembr. 1975, 382, 276-285.
Valiyaveetil, F. I.; MacKinnon, R.; Muir, T. W. Semisynthesis and Folding of the Potassium Channel KcsA. J. Am. Chem. Soc. 2002, 124, 9113-9120.
Shinoda, K.; Yamaguchi, T.; Hori, R. The Surface Tension and the Critical Micelle Concentration in Aqueous Solution of D-Alkyl glucosides and their Mixtures. Bull. Chem. Soc. Jpn. 1961, 34, 237-241.
Drummond, C. J.; Warr, G. G.; Grieser, F.; Ninham, B. W.; Evans, D. F. Surface Properties and Micellar Interfacial Microenvironment of n-Dodecyl D-Maltoside. J. Phys. Chem. 1985, 89, 2103-2109.
Yaseen, M.; Wang, Y.; Su, T. J.; Lu, J. R. Surface Adsorption of Zwitterionic Surfactants: N-Alkyl Phosphocholines Characterised by Surface Tensiometry and Neutron Reflection. J. Colloid Interface Sci. 2005, 288, 361-370.
Rahman, A.; Brown, C. W. Effect of pH on the Critical Micelle Concentration of Sodium Dodecyl Sulphate. J. Appl. Polym. Sci. 1983, 28, 1331-1334.
Kochendoerfer, G. G.; Salom, D.; Lear, J. D.; Wilk-Orescan, R.; Kent, S. B.; DeGrado, W. F. Total Chemical Synthesis of the Integral Membrane Protein Influenza A Virus M2: Role of Its CTerminal Domain in Tetramer Assembly. Biochemistry 1999, 38, 11905-11913.
Sohma, Y.; Kitamura, H.; Kawashima, H.; Hojo, H.; Yamashita, M.; Akaji, K.; Kiso, Y. Synthesis of an O-Acyl Isopeptide by Using Native Chemical Ligation to Efficiently Construct a Hydrophobic Polypeptide. Tetrahedron Lett. 2011, 52, 7146-7148.
Dittmann, M.; Sauermann, J.; Seidel, R.; Zimmermann, W.; Engelhard, M. Native Chemical Ligation of Hydrophobic Peptides in Organic Solvents. J. Pept. Sci. 2010, 16, 558-562.
Dittmann, M.; Sadek, M.; Seidel, R.; Engelhard, M. Native Chemical Ligation in Dimethylformamide Can Be Performed Chemoselectively without Racemization. J. Pept. Sci. 2012, 18, 312-316.
Seebach, D.; Thaler, A.; Beck, A. K. Solubilization of Peptides in Non-Polar Organic Solvents by the Addition of Onorganic Salts: Facts and Implications. Helv. Chim. Acta 1989, 72, 857-867.
Brown, R. S.; Aman, A. Intramolecular Catalysis of Thiol Ester Hydrolysis by a Tertiary Amine and a Carboxylate. J. Org. Chem. 1997, 62, 4816-4820.
Stephenson, R. C.; Clarke, S. Succinimide Formation from Aspartyl and Asparaginyl Peptides as a Model for the Spontaneous Degradation of Proteins. J. Biol. Chem. 1989, 264, 6164-6170.
Behrendt, R.; White, P.; Offer, J. Advances in Fmoc Solid-Phase Peptide Synthesis. J. Pept. Sci. 2016, 22, 4-27.
Jacobsen, M. T.; Erickson, P. W.; Kay, M. S. Aligator: A Computational Tool for Optimizing Total Chemical Synthesis of Large Proteins. Bioorg. Med. Chem. 2017, 25, 4946-4952.
Dang, B.; Dhayalan, B.; Kent, S. B. H. Enhanced Solvation of Peptides Attached to "Solid-Phase" Resins: Straightforward Syntheses of the Elastin Sequence Pro-Gly-Val-Gly-Val-Pro-Gly-Val-Gly-Val. Org. Lett. 2015, 17, 3521-3523.
Galibert, M.; Piller, V.; Piller, F.; Aucagne, V.; Delmas, A. F. Combining Triazole Ligation and Enzymatic Glycosylation on Solid Phase Simplifies the Synthesis of Very Long Glycoprotein Analogues. Chem. Sci. 2015, 6, 3617-3623.
Zitterbart, R.; Seitz, O. Parallel Chemical Protein Synthesis on a Surface Enables the Rapid Analysis of the Phosphoregulation of SH3 Domains. Angew. Chem., Int. Ed. 2016, 55, 7252-7256.
Craik, D. J.; Fairlie, D. P.; Liras, S.; Price, D. The Future of Peptide-Based Drugs. Chem. Biol. Drug Des. 2013, 81, 136-147.
Vlieghe, P.; Lisowski, V.; Martinez, J.; Khrestchatisky, M. Synthetic Therapeutic Peptides: Science and Market. Drug Discov. Drug Discovery Today 2010, 15, 40-56.
Usmani, S. S.; Bedi, G.; Samuel, J. S.; Singh, S.; Kalra, S.; Kumar, P.; Ahuja, A. A.; Sharma, M.; Gautam, A.; Raghava, G. P. S. THPdb: Database of FDA-Approved Peptide and Protein Therapeutics. PLoS One 2017, 12, No. e0181748.
Góngora-Benítez, M.; Tulla-Puche, J.; Albericio, F. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics. Chem. Rev. 2014, 114, 901-926.