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Issue 7, 2006
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Peptide p-nitrophenylanilides containing (E)-dehydrophenylalanine—synthesis, structural studies and evaluation of their activity towards cathepsin C

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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

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Publication details

The article was received on 01 Feb 2006, accepted on 08 May 2006 and first published on 05 Jun 2006


Article type: Paper
DOI: 10.1039/B601634K
Citation: New J. Chem., 2006,30, 1009-1018
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    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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