Peroxides as oxidative enzyme inhibitors: Mechanism-based inhibition of a cysteine protease by an amino acid ozonide

Patrick H. Dussault, A. Denise George, Tony K. Trullinger

Research output: Contribution to journalArticle

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Abstract

A stable ozonide derived from Cbz-L-Phe accomplishes rapid and stoichiometric inhibition of papain at less than 100 μM concentration under conditions where formation of the corresponding aldehyde is negligible. Oxidation of the active site thiolate by the bound peroxide is believed to lead to formation of an inactive sulfenate or sulfenic acid. Reduction of the ozonide in excess DMSO provides a convenient method for in situ generation of a peptide aldehyde.

Original languageEnglish (US)
Pages (from-to)3255-3258
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume9
Issue number22
DOIs
Publication statusPublished - Nov 15 1999

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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