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https://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 |
DOI: | 10.1039/c6ob01159d |
Published version: | http://dx.doi.org/10.1039/c6ob01159d |
Appears in Collections: | Aurora harvest 7 IPAS publications |
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