Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 51, Issue 14, Pages 4346-4350Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm800182c
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Funding
- NCI NIH HHS [R03CA125775, R03 CA125775-02, R03 CA125775] Funding Source: Medline
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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.
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