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Synthesis of Tetrapeptide p‐ nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity
Author(s) -
Makowski Maciej,
Pawełczak Małgorzata,
Latajka Rafał,
Nowak Kornel,
Kafarski Paweł
Publication year - 2001
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.307
Subject(s) - tetrapeptide , dehydroalanine , chemistry , substrate (aquarium) , cathepsin c , cathepsin , biochemistry , peptide , stereochemistry , enzyme , cathepsin d , biology , ecology
Abstract Three dehydrotetrapeptides of rationally varying structure were prepared and tested as affectors of cathepsin C. These compounds appeared to be substrates of the enzyme, being equipotent with their classical counterparts. Thus, replacement of amino acid in a short peptide by corresponding dehydroamino acid does not prevent cathepsin C in recognizing dehydropeptide as its substrate. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.