[en] MALDI in-source decay (ISD) has been used for the top-down sequencing of proteins.
The use of 1,5-diaminonapthalene (1,5-DAN) gave strong intensity of w ions, which are
informative fragments and can be helpful for the distinction of the isobaric amino acids,
Leu and Ile. Our data suggests that the w fragments are formed from z* radical
fragment by unimolecular dissociation and high abundance of w ions in MALDI-ISD
with 1,5-DAN can be understood as resulting from the low collision rate in the MALDI
plume. The MALDI-ISD with 1,5-DAN could be a useful method for the top-down
sequencing of proteins including discrimination of Leu and Ile near the C-terminal end.
Research Center/Unit :
Giga-Systems Biology and Chemical Biology - ULiège
FP7 - 278346 - VENOMICS - High-throughput peptidomics and transcriptomics of animal venoms for discovery of novel therapeutic peptides and innovative drug development
Funders :
F.R.S.-FNRS - Fonds de la Recherche Scientifique JSPS - Japan Society for the Promotion of Science CE - Commission Européenne
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Paizs, B.; Suhai, S.: Fragmentation pathways of protonated peptides. Mass Spectrom. Rev. 24, 508-548 (2005)
Johnson, R.S.; Martin, S.A.; Biemann, K.; Stults, J.T.; Watson, J.T.: Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: differentiation of leucine and isoleucine. Anal. Chem. 59, 2621-2625 (1987)
Zubarev, R.A.: Reactions of polypeptide ions with electrons in the gas phase. Mass Spectrom. Rev. 22, 57-77 (2003)
Syka, J.E.; Coon, J.J.; Schroeder, M.J.; Shabanovitz, J.; Hunt, D.F.: Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc. Natl. Acad. Sci. U.S.A. 101, 9528-9533 (2004)
Kjeldsen, F.; Haselmann, K.F.; Sørensen, E.S.; Zubarev, R.A.: Distinguishing of Ile/Leu amino acid residues in the pp 3 protein by (hot) electron capture dissociation in fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 75, 1267-1274 (2003)
Han, H.; Xia, Y.; McLuckey, S.A.: Ion trap collisional activation of c and z• Ions Formed via Gas-Phase Ion/Ion Electron-Transfer Dissociation. J. Proteome Res. 6, 3062-3069 (2007)
Chung, T.W.; Tureček, F.: Backbone and side-chain specific dissociations of z ions from non-tryptic peptides. J. Am. Soc. Mass Spectrom. 21, 1279-1295 (2010)
Takayama, M.: N-Cα bond cleavage of the peptide backbone via hydrogen abstraction. J. Am. Soc. Mass Spectrom. 12, 1044-1049 (2001)
Köcher, T.; Engström, Å.; Zubarev, R.A.: Fragmentation of peptides in MALDI in-source decay mediated by hydrogen radicals. Anal. Chem. 77, 172-177 (2005)
Hardouin, J.: Protein sequence information by matrix-assisted laser desorption/ionization in-source decay mass spectrometry. Mass Spectrom. Rev. 26, 672-682 (2007)
Sellami, L.; Belgacem, O.; Villard, C.; Openshaw, M.E.; Barbier, P.; Lafitte, D.: In-source decay and pseudo tandem mass spectrometry fragmentation processes of entire high mass proteins on a hybrid vacuum matrix-assisted laser desorption ionization-quadrupole ion-trap time-of-flight mass spectrometer. Anal. Chem. 84, 5180-5185 (2012)
Soltwisch, J.; Dreisewerd, K.: Discrimination of isobaric leucine and isoleucine residues and analysis of post-translational modifications in peptides by MALDI in-source decay mass spectrometry combined with collisional cooling. Anal. Chem. 82, 5628-5635 (2010)
Demeure, K.; Quinton, L.; Gabelica, V.; De Pauw, E.: Rational selection of the optimum MALDI matrix for top-down proteomics by in-source decay. Anal. Chem. 79, 8678-8685 (2007)
Smargiasso, N.; Quinton, L.; De Pauw, E.: 2-Aminobenzamide and 2-aminobenzoic acid as new MALDI matrices inducing radical mediated in-source decay of peptides and proteins. J. Am. Soc. Mass Spectrom. 23, 469-474 (2012)
Demeure, K.; Gabelica, V.; De Pauw, E.: New advances in the understanding of the in-source decay fragmentation of peptides in MALDI-TOF-MS. J. Am. Soc. Mass Spectrom. 21, 1906-1917 (2010)
Spengler, B.; Kirsch, D.: On the formation of initial ion velocities in matrix-assisted laser desorption ionization: Virtual desorption time as an additional parameter describing ion ejection dynamics. Int. J. Mass Spectrom. 226, 71-83 (2003)
Juhasz, P.; Vestal, M.L.; Martin, S.A.: On the initial velocity of ions generated by matrix-assisted laser desorption ionization and its effect on the calibration of delayed extraction time-of-flight mass spectra. J. Am. Soc. Mass Spectrom. 8, 209-217 (1997)
Asakawa, D.; Takayama, M.: Cα-C bond cleavage of the peptide backbone in MALDI in-source decay using salicylic acid derivative matrices. J. Am. Soc. Mass Spectrom. 22, 1224-1233 (2011)
Asakawa, D.; Takayama, M.: Fragmentation processes of hydrogen-deficient peptide radicals in matrix-assisted laser desorption/ionization in-source decay mass spectrometry. J. Phys. Chem. B 116, 4016-4023 (2012)
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.