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|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|
|Citation:||Organic and Biomolecular Chemistry, 2016; 14(29):6970-6978|
|Publisher:||Royal Society of Chemistry|
|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|
|Appears in Collections:||IPAS publications|
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