Pentapeptides containing two dehydrophenylalanine residues--synthesis, structural studies and evaluation of their activity towards cathepsin C

Autor:	Latajka, R., Jewginski, M., Makowski, M., Paweiczak, M., Huber, T., Sewald, Norbert, Kafarski, P.
Rok vydání:	2008
Předmět:	conformation Models Molecular dehydropeptide Magnetic Resonance Spectroscopy Phenylalanine Protease Inhibitors inhibitors of cathepsin C Binding Competitive Oligopeptides Cathepsin C Protein Structure Secondary Substrate Specificity
Zdroj:	Journal of peptide science : an official publication of the European Peptide Society. 14(10)
ISSN:	1075-2617
Popis:	Synthesis, structural and biological studies of pentapeptides containing two Delta Phe residues (Z and E isomers) in position 2 and 4 in peptide chain were performed. All the investigated peptides adopted bent conformation and majority of them could exist as two different. conformers in solution. Only pentapeptides. containing free N-termini appeared to act as weak inhibitors of cathepsin C with the slow-binding, competitive mechanism of inhibition. free acids being bound slightly better than their methyl esters. Results of Molecular modeling suggested significant difference between peptides, depending of the type of amino acid residue in position 5 in peptide chain. Dehydropeptides containing GIN, residue in this position may act as competitive slow-reacting substrates and therefore exhibit inhibitory-like properties. Copyright (C) 2008 European Peptide Society and John Wiley & Sons, Ltd.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f697c59bec2a1aafd2a0f065771b3714 https://pubmed.ncbi.nlm.nih.gov/18523964 Zobrazit plný text záznamu Plný text