Abstract
Starting from the purine lead structure 1, a new series of cathepsin K inhibitors based on a pyrimidine scaffold have been explored. Investigations of P3 and P2 substituents based on molecular modeling suggestions resulted in potent cathepsin K inhibitors with an improved selectivity profile over other cathepsins.
MeSH terms
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Animals
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Binding Sites
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Cathepsin K
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Cathepsins / antagonists & inhibitors*
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Cathepsins / chemistry*
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Crystallography, X-Ray
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Cysteine Endopeptidases / chemistry*
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Models, Molecular*
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Nitriles / chemical synthesis*
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Nitriles / chemistry
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Nitriles / pharmacokinetics
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Protease Inhibitors / chemical synthesis*
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Protease Inhibitors / chemistry
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Protease Inhibitors / pharmacokinetics
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Pyrimidines / chemical synthesis*
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Pyrimidines / chemistry
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Pyrimidines / pharmacokinetics
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Rats
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Structure-Activity Relationship
Substances
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Nitriles
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Protease Inhibitors
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Pyrimidines
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Cathepsins
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Cysteine Endopeptidases
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Cathepsin K
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Ctsk protein, rat