Abstract
A series of dipeptidyl nitriles as inhibitors of cathepsin K have been explored starting from lead structure 1 (Cbz-Leu-NH-CH2-CN, IC50 = 39 nM). Attachment of non-natural amino acid side chains in P1 and modification of the P3 subunit led to inhibitors with higher potency and improved pharmacokinetic properties.
MeSH terms
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Animals
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Cathepsin K
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Cathepsins / antagonists & inhibitors*
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Cathepsins / metabolism
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Dipeptides / chemical synthesis
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Dipeptides / chemistry
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Dipeptides / pharmacology*
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Drug Evaluation, Preclinical
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Humans
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In Vitro Techniques
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Microsomes, Liver / drug effects
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Microsomes, Liver / enzymology
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Microsomes, Liver / metabolism
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Molecular Structure
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Nitriles / chemical synthesis
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Nitriles / chemistry
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Nitriles / pharmacology*
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Rats
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Stereoisomerism
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Structure-Activity Relationship
Substances
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Dipeptides
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Enzyme Inhibitors
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Nitriles
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Cathepsins
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CTSK protein, human
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Cathepsin K
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Ctsk protein, rat