Kojima M., Hosoda H., Date Y., Nakazato M., Matsuo H., Kangawa K. Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature 1999, 402:656-660.
Hosoda H., Kojima M., Mizushima T., Shimizu S., Kangawa K. Structural divergence of human ghrelin. Identification of multiple ghrelin-derived molecules produced by post-translational processing. J. Biol. Chem. 2003, 278:64-70.
Gutierrez J.A., Solenberg P.J., Perkins D.R., Willency J.A., Knierman M.D., Jin Z., Witcher D.R., Luo S., Onyia J.E., Hale J.E. Ghrelin octanoylation mediated by an orphan lipid transferase. Proc. Natl. Acad. Sci. U. S. A 2008, 105:6320-6325.
Yang J., Brown M.S., Liang G., Grishin N.V., Goldstein J.L. Identification of the acyltransferase that octanoylates ghrelin, an appetite-stimulating peptide hormone. Cell 2008, 132:387-396.
Kojima M., Kangawa K. Ghrelin: structure and function. Physiol. Rev. 2005, 85:495-522.
Leite-Moreira A.F., Soares J.B. Physiological, pathological and potential therapeutic roles of ghrelin. Drug Discov. Today 2007, 12:276-288.
Soares J.B., Leite-Moreira A.F. Ghrelin, des-acyl ghrelin and obestatin: three pieces of the same puzzle. Peptides 2008, 29:1255-1270.
Gauna C., van de Zande B., van Kerkwijk A., Themmen A.P., van der Lely A.J., Delhanty P.J. Unacylated ghrelin is not a functional antagonist but a full agonist of the type 1a growth hormone secretagogue receptor (GHS-R). Mol. Cell. Endocrinol. 2007, 274:30-34.
Sargent D.F., Schwyzer R. Membrane lipid phase as catalyst for peptide-receptor interactions. Proc. Natl. Acad. Sci. U. S. A 1986, 83:5774-5778.
Castanho M.A., Fernandes M.X. Lipid membrane-induced optimization for ligand-receptor docking: recent tools and insights for the "membrane catalysis" model. Eur. Biophys. J. 2006, 35:92-103.
Schwyzer R. 100years lock-and-key concept: are peptide keys shaped and guided to their receptors by the target cell membrane?. Biopolymers 1995, 37:5-16.
Seelig J. Titration calorimetry of lipid-peptide interactions. Biochim. Biophys. Acta 1997, 1331:103-116.
Seelig J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 2004, 1666:40-50.
Dehlin E., Liu J., Yun S.H., Fox E., Snyder S., Gineste C., Willingham L., Geysen M., Gaylinn B.D., Sando J.J. Regulation of ghrelin structure and membrane binding by phosphorylation. Peptides 2008, 29:904-911.
Banks W.A., Tschop M., Robinson S.M., Heiman M.L. Extent and direction of ghrelin transport across the blood-brain barrier is determined by its unique primary structure. J. Pharmacol. Exp. Ther. 2002, 302:822-827.
Staes E., Rozet E., Ucakar B., Hubert P., Préat V. Validation of a method for the quantitation of ghrelin and unacylated ghrelin by HPLC. J. Pharm. Biomed. Anal. 2010, 51:633-639.
Asada H., Douen T., Waki M., Adachi S., Fujita T., Yamamoto A., Muranishi S. Absorption characteristics of chemically modified-insulin derivatives with various fatty acids in the small and large intestine. J. Pharm. Sci. 1995, 84:682-687.
Fujita T., Kawahara I., Quan Y., Hattori K., Takenaka K., Muranishi S., Yamamoto A. Permeability characteristics of tetragastrins across intestinal membranes using the Caco-2 monolayer system: comparison between acylation and application of protease inhibitors. Pharm. Res. 1998, 15:1387-1392.
Hope M.J., Bally M.B., Webb G., Cullis P.R. Production of large unilamellar vesicles by a rapid extrusion procedure. Characterization of size distribution, trapped volume and ability to maintain a membrane potential. Biochim. Biophys. Acta 1985, 812:55-65.
Mathot F., Schanck A., Van Bambeke F., Arien A., Noppe M., Brewster M., Préat V. Passive diffusion of polymeric surfactants across lipid bilayers. J. Control. Release 2007, 120:79-87.
Bartlett G.R. Phosphorus assay in column chromatography. J. Biol. Chem. 1959, 234:466-468.
Chanteux H., Paternotte I., Mingeot-Leclercq M.P., Brasseur R., Sonveaux E., Tulkens P.M. Cell handling, membrane-binding properties, and membrane-penetration modeling approaches of pivampicillin and phthalimidomethylampicillin, two basic esters of ampicillin, in comparison with chloroquine and azithromycin. Pharm. Res. 2003, 20:624-631.
Shinitzky M., Barenholz Y. Dynamics of the hydrocarbon layer in liposomes of lecithin and sphingomyelin containing dicetylphosphate. J. Biol. Chem. 1974, 249:2652-2657.
Mingeot-Leclercq M.P., Lins L., Bensliman M., Van Bambeke F., Van Der Smissen P., Peuvot J., Schanck A., Brasseur R. Membrane destabilization induced by beta-amyloid peptide 29-42: importance of the amino-terminus. Chem. Phys. Lipids 2002, 120:57-74.
Andrushchenko V.V., Vogel H.J., Prenner E.J. Optimization of the hydrochloric acid concentration used for trifluoroacetate removal from synthetic peptides. J. Pept. Sci. 2007, 13:37-43.
Haris P.I., Chapman D. The conformational analysis of peptides using Fourier transform IR spectroscopy. Biopolymers 1995, 37:251-263.
Lins L., Brasseur R. Tilted peptides: a structural motif involved in protein membrane insertion?. J. Pept. Sci. 2008, 14:416-422.
Goormaghtigh E., Raussens V., Ruysschaert J.M. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1999, 1422:105-185.
Lins L., Brasseur R., Rosseneu M., Yang C.Y., Sparrow D.A., Sparrow J.T., Gotto A.M., Ruysschaert J.M. Structure and orientation of apo B-100 peptides into a lipid bilayer. J. Protein Chem. 1994, 13:77-88.
Thomas A., Deshayes S., Decaffmeyer M., Van Eyck M.H., Charloteaux B., Brasseur R. Prediction of peptide structure: how far are we?. Proteins 2006, 65:889-897.
Lagarias J.C., Reeds J.A., Wright M.H., Wright P.E. Convergence properties of the Nelder-Mead simplex method in low dimensions. SIAM J. Optim. 1998, 9:112-147.
Nelder J.A., Mead R. A simplex method for function minimazation. Comput. J. 1965, 7:308-313.
Wiseman T., Williston S., Brandts J.F., Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 1989, 179:131-137.
Ziegler A., Blatter X.L., Seelig A., Seelig J. Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis. Biochemistry 2003, 42:9185-9194.
Beschiaschvili G., Seelig J. Peptide binding to lipid bilayers. Binding isotherms and zeta-potential of a cyclic somatostatin analogue. Biochemistry 1990, 29:10995-11000.
Wieprecht T., Seelig J. Isothermal titration calorimetry for studying interactions between peptides and lipid membranes. Current topics in membranes 2002, vol. 52:31-56. Academic Press, San Diego, California. S.A. Simon, T.J. McIntosh (Eds.).
McLaughlin S. Electrostatic potentials at membrane-solution interfaces. Current Topics in Membranes and Transport 1977, Vol. 9:71-144. Academic Press, New York. F. Bronner, A. Kleinzeller (Eds.).
Delgado A.V., Gonzalez-Caballero F., Hunter R.J., Koopal L.K., Lyklema J. Measurement and interpretation of electrokinetic phenomena. J. Colloid Interface Sci. 2007, 309:194-224.
Rasmusson M. Polymer particles and polyelectrolytes: surface electrical properties. Encyclopedia of Surface and Colloid Science 2006, 4900-4920. Taylor & Francis, London. P. Somasundaran, A. Hubbard (Eds.).
Hiemenz P.C., Rajagopalan R. Principles of Colloid and Surface Chemistry 1997, Marcel Dekker, New York. 3rd.
Seelig A. Local anesthetics and pressure: a comparison of dibucaine binding to lipid monolayers and bilayers. Biochim. Biophys. Acta 1987, 899:196-204.
Ruso J.M., Besada L., Martinez-Landeira P., Seoane L., Prieto G., Sarmiento F. Interactions between liposomes and cations in aqueous solution. J. Liposome Res. 2003, 13:131-145.
McLaughlin S. The electrostatic properties of membranes. Annu. Rev. Biophys. Biophys. Chem. 1989, 18:113-136.
Klocek G., Schulthess T., Shai Y., Seelig J. Thermodynamics of melittin binding to lipid bilayers. Aggregation and pore formation. Biochemistry 2009, 48:2586-2596.
Matos C., de Castro B., Gameiro P., Lima J.L., Reis S. Zeta-potential measurements as a tool to quantify the effect of charged drugs on the surface potential of egg phosphatidylcholine liposomes. Langmuir 2004, 20:369-377.
des Rieux A., Ragnarsson E.G., Gullberg E., Préat V., Schneider Y.J., Artursson P. Transport of nanoparticles across an in vitro model of the human intestinal follicle associated epithelium. Eur. J. Pharm. Sci. 2005, 25:455-465.
des Rieux A., Fievez V., Théate I., Mast J., Préat V., Schneider Y.J. An improved in vitro model of human intestinal follicle-associated epithelium to study nanoparticle transport by M cells. Eur. J. Pharm. Sci. 2007, 30:380-391.
Cunderlikova B., Moan J. Electrostatic properties of cells estimated by absorption and fluorescence spectroscopy. Cell Biochem. Biophys. 2004, 41:1-10.
Wall J., Ayoub F., O'Shea P. Interactions of macromolecules with the mammalian cell surface. J. Cell Sci. 1995, 108(Pt 7):2673-2682.
Zachowski A. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. J. 1993, 294:1-14.
Beaumont N.J., Skinner V.O., Tan T.M., Ramesh B.S., Byrne D.J., MacColl G.S., Keen J.N., Bouloux P.M., Mikhailidis D.P., Bruckdorfer K.R., Vanderpump M.P., Srai K.S. Ghrelin can bind to a species of high density lipoprotein associated with paraoxonase. J. Biol. Chem. 2003, 278:8877-8880.
De Vriese C., Hacquebard M., Gregoire F., Carpentier Y., Delporte C. Ghrelin interacts with human plasma lipoproteins. Endocrinology 2007, 148:2355-2362.
Lockridge O., Xue W., Gaydess A., Grigoryan H., Ding S.J., Schopfer L.M., Hinrichs S.H., Masson P. Pseudo-esterase activity of human albumin: slow turnover on tyrosine 411 and stable acetylation of 82 residues including 59 lysines. J. Biol. Chem. 2008, 283:22582-22590.
De Vriese C., Gregoire F., Lema-Kisoka R., Waelbroeck M., Robberecht P., Delporte C. Ghrelin degradation by serum and tissue homogenates: identification of the cleavage sites. Endocrinology 2004, 145:4997-5005.
Sedlackova D., Dostalova I., Hainer V., Beranova L., Kvasnickova H., Hill M., Haluzik M., Nedvidkova J. Simultaneous decrease of plasma obestatin and ghrelin levels after a high-carbohydrate breakfast in healthy women. Physiol. Res. 2008, 57(Suppl 1):S29-S37.
Machaidze G., Seelig J. Specific binding of cinnamycin (Ro 09-0198) to phosphatidylethanolamine. Comparison between micellar and membrane environments. Biochemistry 2003, 42:12570-12576.
DiNitto J.P., Cronin T.C., Lambright D.G. Membrane recognition and targeting by lipid-binding domains. Sci. STKE 2003, 2003:re16.
Cevc G. Phospholipids Handbook 1993, Marcel Dekker, Inc, New York.
Montich G., Scarlata S., McLaughlin S., Lehrmann R., Seelig J. Thermodynamic characterization of the association of small basic peptides with membranes containing acidic lipids. Biochim. Biophys. Acta 1993, 1146:17-24.
Seelig A., Blatter X.L., Frentzel A., Isenberg G. Phospholipid binding of synthetic talin peptides provides evidence for an intrinsic membrane anchor of talin. J. Biol. Chem. 2000, 275:17954-17961.
Wenk M.R., Seelig J. Magainin 2 amide interaction with lipid membranes: calorimetric detection of peptide binding and pore formation. Biochemistry 1998, 37:3909-3916.
Bednarek M.A., Feighner S.D., Pong S.S., McKee K.K., Hreniuk D.L., Silva M.V., Warren V.A., Howard A.D., Van Der Ploeg L.H., Heck J.V. Structure-function studies on the new growth hormone-releasing peptide, ghrelin: minimal sequence of ghrelin necessary for activation of growth hormone secretagogue receptor 1a. J. Med. Chem. 2000, 43:4370-4376.
Arseneault M., Lafleur M. Isothermal titration calorimetric study of calcium association to lipid bilayers: influence of the vesicle preparation and composition. Chem. Phys. Lipids 2006, 142:84-93.
Charlton I.D., Doherty A.P. Locating the micellar shear plane and its relationship with the Debye screening length. J. Phys. Chem. B 1999, 103:5081-5083.
Yang Z., Zhao J., Lu Y., Du Z., Yang Z. Ultramicroelectrode voltammetric measurement of the hydrodynamic radii and shear plane of micellar particles for sodium dodecylsulfonate in aqueous NaCl solution. Chem. Phys. 2004, 307:71-75.
Binder H., Lindblom G. Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys. J. 2003, 85:982-995.
Seelig J., Nebel S., Ganz P., Bruns C. Electrostatic and nonpolar peptide-membrane interactions. Lipid binding and functional properties of somatostatin analogues of charge z = +1 to z = +3. Biochemistry 1993, 32:9714-9721.
Hanakam F., Gerisch G., Lotz S., Alt T., Seelig A. Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch. Biochemistry 1996, 35:11036-11044.
Peitzsch R.M., McLaughlin S. Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins. Biochemistry 1993, 32:10436-10443.
Simon S.A., McIntosh T.J. Peptide-lipid interactions 2002, Academic Press, San Diego, Calif.
Kaiser R.D., London E. Location of diphenylhexatriene (DPH) and its derivatives within membranes: comparison of different fluorescence quenching analyses of membrane depth. Biochemistry 1998, 37:8180-8190.
Beevers A.J., Kukol A. Conformational flexibility of the peptide hormone ghrelin in solution and lipid membrane bound: a molecular dynamics study. J. Biomol. Struct. Dyn. 2006, 23:357-364.
Dike A., Cowsik S.M. Membrane-induced structure of scyliorhinin I: a dual NK1/NK2 agonist. Biophys. J. 2005, 88:3592-3600.
Satheeshkumar K.S., Jayakumar R. Conformational polymorphism of the amyloidogenic peptide homologous to residues 113-127 of the prion protein. Biophys. J. 2003, 85:473-483.
Sui S.F. Membrane-induced conformational change of proteins. Adv. Colloid Interface Sci. 2000, 85:257-267.
Chopineau J., Robert S., Fenart L., Cecchelli R., Lagoutte B., Paitier S., Dehouck M.P., Domurado D. Monoacylation of ribonuclease A enables its transport across an in vitro model of the blood-brain barrier. J. Control. Release 1998, 56:231-237.
Harishchandran A., Nagaraj R. Interaction of a pseudosubstrate peptide of protein kinase C and its myristoylated form with lipid vesicles: only the myristoylated form translocates into the lipid bilayer. Biochim. Biophys. Acta 2005, 1713:73-82.
Yamamoto A. Improvement of intestinal absorption of peptide and protein drugs by chemical modification with fatty acids. Nippon Rinsho 1998, 56:601-607.
des Rieux A., Fievez V., Momtaz M., Detrembleur C., Alonso-Sande M., Van Gelder J., Cauvin A., Schneider Y.J., Préat V. Helodermin-loaded nanoparticles: characterization and transport across an in vitro model of the follicle-associated epithelium. J. Control. Release 2007, 118:294-302.
Lopes S.C., Fedorov A., Castanho M.A. Lipidic membranes are potential "catalysts" in the ligand activity of the multifunctional pentapeptide neokyotorphin. Chem. Biochem. 2005, 6:697-702.
Matsumoto M., Hosoda H., Kitajima Y., Morozumi N., Minamitake Y., Tanaka S., Matsuo H., Kojima M., Hayashi Y., Kangawa K. Structure-activity relationship of ghrelin: pharmacological study of ghrelin peptides. Biochem. Biophys. Res. Commun. 2001, 287:142-146.
Kojima M., Kangawa K. Structure and function of ghrelin. Results Probl. Cell Differ. 2008, 46:89-115.
Holst B., Holliday N.D., Bach A., Elling C.E., Cox H.M., Schwartz T.W. Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 2004, 279:53806-53817.
Holst B., Lang M., Brandt E., Bach A., Howard A., Frimurer T.M., Beck-Sickinger A., Schwartz T.W. Ghrelin receptor inverse agonists: identification of an active peptide core and its interaction epitopes on the receptor. Mol. Pharmacol. 2006, 70:936-946.
Holst B., Mokrosinski J., Lang M., Brandt E., Nygaard R., Frimurer T.M., Beck-Sickinger A.G., Schwartz T.W. Identification of an efficacy switch region in the ghrelin receptor responsible for interchange between agonism and inverse agonism. J. Biol. Chem. 2007, 282:15799-15811.
Liu G., Fortin J.P., Beinborn M., Kopin A.S. Four missense mutations in the ghrelin receptor result in distinct pharmacological abnormalities. J. Pharmacol. Exp. Ther. 2007, 322:1036-1043.
Pantel J., Legendre M., Cabrol S., Hilal L., Hajaji Y., Morisset S., Nivot S., Vie-Luton M.P., Grouselle D., de Kerdanet M., Kadiri A., Epelbaum J., Le B.Y., Amselem S. Loss of constitutive activity of the growth hormone secretagogue receptor in familial short stature. J. Clin. Invest. 2006, 116:760-768.
Zhang W., Crocker E., McLaughlin S., Smith S.O. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. J. Biol. Chem. 2003, 278:21459-21466.