Abstract
Four new peptidyl aldehydes bearing proline mimetics at the P(2)-position were synthesized and studied as inhibitors of calpain I, cathepsin B, and selected serine proteases. The ring size of the P(2)-constraining residue influenced the inhibitory potency and selectivity of the compounds for calpain I compared to the other proteases.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aldehydes / chemical synthesis
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Aldehydes / pharmacology*
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Animals
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Biomimetic Materials / chemical synthesis
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Biomimetic Materials / pharmacology*
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Calpain / antagonists & inhibitors*
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Cathepsin B / antagonists & inhibitors
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Cysteine Proteinase Inhibitors / chemical synthesis
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Cysteine Proteinase Inhibitors / pharmacology*
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Humans
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Liver / enzymology
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Oligopeptides / chemical synthesis
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Oligopeptides / pharmacology*
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Proline / chemistry*
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Serine Proteinase Inhibitors / chemical synthesis
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Serine Proteinase Inhibitors / pharmacology*
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Stereoisomerism
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Structure-Activity Relationship
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Swine
Substances
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Aldehydes
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Cysteine Proteinase Inhibitors
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Oligopeptides
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Serine Proteinase Inhibitors
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Proline
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Calpain
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Cathepsin B