Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/51816
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: D-Leu-L-Phe-containing dipeptide inhibitors of -chymosrypsin- the role of the N- and C-termini in enzyme affinity
Author: Pearson, D.
Abell, A.
Citation: ARKIVOC, 2008; 2008(12):85-93
Publisher: Arkat USA, Inc.
Issue Date: 2008
ISSN: 1551-7004
1551-7012
Statement of
Responsibility: 
David Pearson and Andrew D. Abell
Abstract: Three new compounds (3-5) based on a dipeptide non-covalent inhibitor (1) of α-chymotrypsin have been synthesised and assayed against the serine protease α-chymotrypsin. The stability of the compounds to α-chymotrypsin catalysed hydrolysis has been measured. All three compounds were inactive with a retained stability to enzyme catalysed hydrolysis.
Keywords: Chymotrypsin
enzyme inhibitors
peptidomimetics
azobenzene
DOI: 10.3998/ark.5550190.0009.c10
Published version: http://www.arkat-usa.org/arkivoc-journal/browse-arkivoc/2008/12/
Appears in Collections:Aurora harvest
Chemistry and Physics publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.