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

Jim Iley, Rui Moreira, Luísa Martins, Rita C. Guedes, Cláudio M. Soares

Research output: Contribution to journalArticle

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2738-2741
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume16
Issue number10
DOIs
Publication statusPublished - 15 May 2006

Keywords

  • Bsmoc
  • Cathepsin B
  • Cysteine proteases
  • Papain

Fingerprint Dive into the research topics of 'The Bsmoc group as a novel scaffold for the design of irreversible inhibitors of cysteine proteases'. Together they form a unique fingerprint.

  • Cite this