Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/101279
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Type: Journal article
Title: A mechanistic study on the inhibition of α-chymotrypsin by a macrocyclic peptidomimetic aldehyde
Other Titles: A mechanistic study on the inhibition of alpha-chymotrypsin by a macrocyclic peptidomimetic aldehyde
Author: Zhang, X.
Bruning, J.
George, J.
Abell, A.
Citation: Organic and Biomolecular Chemistry, 2016; 14(29):6970-6978
Publisher: Royal Society of Chemistry
Issue Date: 2016
ISSN: 1477-0520
1477-0539
Statement of
Responsibility: 
X. Zhang, J. B. Bruning, J. H. George and A. D. Abell
Abstract: Here we describe an NMR and X-ray crystallography-based characterisation of the mechanism by which a new class of macrocyclic peptidomimetic aldehyde inhibits α-chymotrypsin. In particular, a (13)C-labelled analogue of the inhibitor was prepared and used in NMR experiments to confirm formation of a hemiacetal intermediate on binding with α-chymotrypsin. Analysis of an X-ray crystallographic structure in complex with α-chymotrypsin reveals that the backbone adopts a stable β-strand conformation as per its design. Binding is further stabilised by interaction with the oxyanion hole near the S1 subsite and multiple hydrogen bonds.
Keywords: Aldehydes; Macrocyclic Compounds; Chymotrypsin; Enzyme Inhibitors; Crystallography, X-Ray; Magnetic Resonance Spectroscopy; Molecular Structure; Models, Molecular; Peptidomimetics
Description: First published online 23 Jun 2016
Rights: This journal is © The Royal Society of Chemistry 2016
RMID: 0030050142
DOI: 10.1039/c6ob01159d
Appears in Collections:IPAS publications

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