Issue 7, 2006

Peptide p-nitrophenylanilides containing (E)-dehydrophenylalanine—synthesis, structural studies and evaluation of their activity towards cathepsin C

Abstract

Tetrapeptide p-nitroanilides containing (E)-dehydrophenylalanine were synthesized and evaluated as inhibitors and substrates of cathepsin C. Peptides containing a free, unblocked amino group appeared to be quite good substrates of the enzyme, whereas fully protected peptides acted as very weak inhibitors. Structural studies by means of NMR and CD, alongside with molecular modelling, have proved that these peptides are hydrolysed in one step by direct removal of p-nitroaniline from the tetrapeptide.

Graphical abstract: Peptide p-nitrophenylanilides containing (E)-dehydrophenylalanine—synthesis, structural studies and evaluation of their activity towards cathepsin C

Supplementary files

Article information

Article type
Paper
Submitted
01 Feb 2006
Accepted
08 May 2006
First published
05 Jun 2006

New J. Chem., 2006,30, 1009-1018

Peptide p-nitrophenylanilides containing (E)-dehydrophenylalanine—synthesis, structural studies and evaluation of their activity towards cathepsin C

R. Latajka, M. Makowski, M. Jewgiński, M. Pawełczak, H. Koroniak and P. Kafarski, New J. Chem., 2006, 30, 1009 DOI: 10.1039/B601634K

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