The Bsmoc group as a novel scaffold for the design of irreversible inhibitors of cysteine proteases

Iley, Jim; Moreira, Rui; Martins, Luisa; Guedes, Rita C. and Soares, Claudio M. (2006). The Bsmoc group as a novel scaffold for the design of irreversible inhibitors of cysteine proteases. Bioorganic and Medicinal Chemistry Letters, 16(10) 2738 -2741.

DOI (Digital Object Identifier) Link:	http://dx.doi.org/10.1016/j.bmcl.2006.02.007

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Abstract

Carbamate and ester derivatives of the 1,1-dioxobenzo[b]thiophen-2-ylmethyloxycarbonyl (Bsmoc) scaffold react readily with thiols via a Michael addition at rates not significantly affected by the nature of the carboxylic or carbamic acid leaving group. These Michael acceptors are irreversible inhibitors of the cysteine proteases papain and human liver cathepsin B, displaying first order kinetics with respect to inhibitor concentration. In contrast, none of the Bsmoc derivatives inhibited porcine pancreatic elastase, a serine protease.

Item Type:	Journal Article
ISSN:	0960-894X
Extra Information:	This item is in the 'short communications' section of the journal. Some of the symbols may not have transferred correctly into this bibliographic record.
Keywords:	BSMOC; Papain; Cathepsin B; Cysteine proteases
Academic Unit/Department:	Science > Life, Health and Chemical Sciences
Item ID:	3984
Depositing User:	James Iley
Date Deposited:	04 Jul 2006
Last Modified:	02 Dec 2010 19:50
URI:	http://oro.open.ac.uk/id/eprint/3984

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