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

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.

SUBMITTER: Donkor IO

PROVIDER: S-EPMC2643072 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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

Donkor Isaac O IO Assefa Haregewein H Liu Jiuyu J

Journal of medicinal chemistry 20080701 14

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. ...[more]

PMID: 18636690

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