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J Med Chem. 2008 Jul 24;51(14):4346-50. doi: 10.1021/jm800182c.

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

Author information

1
Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA. idonkor@utmem.edu

Abstract

A series of peptidyl alpha-ketoacids and alpha-ketoesters was synthesized and studied as mu-calpain inhibitors. Docking studies revealed that the mu-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 S 3 pocket of the enzyme.

PMID:
18636690
PMCID:
PMC2643072
DOI:
10.1021/jm800182c
[Indexed for MEDLINE]
Free PMC Article

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