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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Acids / chemistry*
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Acids / pharmacology*
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Calpain / antagonists & inhibitors*
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Cysteine Proteinase Inhibitors / chemistry*
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Cysteine Proteinase Inhibitors / pharmacology*
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Hydrogen Bonding
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Structure
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Peptides / chemistry*
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Spectrometry, Mass, Electrospray Ionization
Substances
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Acids
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Cysteine Proteinase Inhibitors
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Peptides
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Calpain