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

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 dehydroami...

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Bibliographic Details
Published in:Journal of peptide science 2001-03, Vol.7 (3), p.141-145
Main Authors: Makowski, Maciej, Pawełczak, Małgorzata, Latajka, Rafał, Nowak, Kornel, Kafarski, Paweł
Format: Article
Language:English
Subjects:
Alanine - analogs & derivatives
Alanine - chemistry
Amino Acids - chemistry
Anilides - chemical synthesis
Anilides - chemistry
Animals
Cathepsin C - chemistry
Cathepsin C - metabolism
Cattle
dehydroamino acids
dipeptidyl-peptidase I
Magnetic Resonance Spectroscopy
Models, Chemical
Oligopeptides - chemical synthesis
Oligopeptides - chemistry
Phenylalanine - analogs & derivatives
Phenylalanine - chemistry
proteolytic enzymes
Spleen - metabolism
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Summary: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.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.307