Structural basis for the potent calpain inhibitory activity of peptidyl α-ketoacids

Isaac Donkor, Haregewein Assefa, Jiuyu Liu

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A series of peptidyl α-ketoacids and α-ketoesters was synthesized and studied as μ-calpain inhibitors. Docking studies revealed that the μ-calpain inhibitory activity of the compounds is influenced by hydrogen bonding interactions and the potential for ionic interaction with active site residues as well as placement of a planar N-terminal capping group into the S3 pocket of the enzyme.

Original languageEnglish (US)
Pages (from-to)4346-4350
Number of pages5
JournalJournal of Medicinal Chemistry
Volume51
Issue number14
DOIs
StatePublished - Jul 24 2008

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Calpain
Hydrogen Bonding
Catalytic Domain
Enzymes
calpain inhibitors

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Drug Discovery

Cite this

Structural basis for the potent calpain inhibitory activity of peptidyl α-ketoacids. / Donkor, Isaac; Assefa, Haregewein; Liu, Jiuyu.

In: Journal of Medicinal Chemistry, Vol. 51, No. 14, 24.07.2008, p. 4346-4350.

Research output: Contribution to journalArticle

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