Peptide methyl ketones as reversible inhibitors of cysteine proteinases

Dieter Brömme, Beate Bartels, Heidrun Kirschke, Siegfried Fittkau

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17 Scopus citations


Peptide methyl ketones represent a new class of reversible, competitive cysteine proteinase inhibitor with little or no effect on serine proteinases. The affinity of the inhibitors to papain (EC, cathepsin B (EC and cathepsin L (EC depends on the peptide chain length and on side-chain effects. Variations in the P1 and P4 positions (terminology of Schechter and Berger1) and their influence on the efficiency of the inhibitors have been investigated. The most effective inhibitors display inhibition constants in the micromolar range. In contrast to the endopeptidases papain and the cathepsins B and L, the aminoendopeptidase cathepsin H (EC is not inhibited by N-acylated peptide methyl ketones but only by amino methyl ketones containing a free a-amino group. The endopeptidases are not affected by amino methyl ketones.

Original languageEnglish
Pages (from-to)13-21
Number of pages9
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Issue number1
StatePublished - 1989
Externally publishedYes


  • Cathepsin B
  • Cathepsin H
  • Cathepsin L
  • Competitive inhibitors
  • Papain
  • Peptide methyl ketones


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