Abstract
A modification of novel cathepsin K inhibitors I was carried out. The structural design was aimed at reducing the lipophilic character of compounds I for obtaining better pharmacokinetic profiles. This modification afforded several less lipophilic compounds with good inhibitory activities and pharmacokinetic profiles, although the enzyme selectivity over cathepsin S was left at issue.
MeSH terms
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Amines / chemical synthesis
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Amines / chemistry
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Amines / pharmacology*
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Cathepsin B / antagonists & inhibitors
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Cathepsin K
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Cathepsin L
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Cathepsins / antagonists & inhibitors*
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Cysteine Endopeptidases
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Enzyme Activation / drug effects
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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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Heterocyclic Compounds / chemical synthesis
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Heterocyclic Compounds / chemistry
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Heterocyclic Compounds / pharmacology*
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Humans
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Molecular Conformation
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Recombinant Proteins / antagonists & inhibitors
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Stereoisomerism
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Structure-Activity Relationship
Substances
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Amines
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Enzyme Inhibitors
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Heterocyclic Compounds
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Recombinant Proteins
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Cathepsins
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Cysteine Endopeptidases
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Cathepsin B
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CTSL protein, human
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Cathepsin L
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cathepsin S
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CTSK protein, human
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Cathepsin K