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

5 Citations (Scopus)

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
StatePublished - Nov 15 1999

Fingerprint

Cysteine Proteases
Peroxides
Enzyme Inhibitors
Aldehydes
Sulfenic Acids
Amino Acids
Papain
Dimethyl Sulfoxide
Catalytic Domain
Oxidation
Peptides
1,2,4-trioxane

ASJC Scopus subject areas

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

Cite this

Peroxides as oxidative enzyme inhibitors : Mechanism-based inhibition of a cysteine protease by an amino acid ozonide. / Dussault, Patrick H.; George, A. Denise; Trullinger, Tony K.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 9, No. 22, 15.11.1999, p. 3255-3258.

Research output: Contribution to journalArticle

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