Synthesis of tetrapeptide p-nitrophenylanilides containing dehydroalanine and dehydrophenylalanine and their influence on cathepsin C activity

Three dehydrotetrapeptides of rationally varying structure were prepared an d tested as affectors of cathepsin C. These compounds appeared to be substr ates of the enzyme, being equipotent with their classical counterparts. Thu s, replacement of amino acid in a short peptide by corresponding dehydroami no acid does not prevent cathepsin C in recognizing dehydropeptide as its s ubstrate. Copyright (C) 2001 European Peptide Society and John Wiley & Sons , Ltd.