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• W2044280138 abstract "Using the example of cathepsin K, we demonstrate the design of highly potent and selective azadipeptide nitrile inhibitors. A systematic scan with respect to P2 and P3 substituents was carried out. Structural modifications strongly affected the enzyme−inhibitor association (but not dissociation) rate. A combination of optimized P2 and P3 substituents with a methylation of the P3−P2 amide linker resulted in the picomolar cathepsin K inhibitor 19 with remarkable selectivity over cathepsins L, B, and S." @default.
• W2044280138 created "2016-06-24" @default.
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• W2044280138 date "2010-12-03" @default.
• W2044280138 modified "2023-09-25" @default.
• W2044280138 title "Structural Optimization of Azadipeptide Nitriles Strongly Increases Association Rates and Allows the Development of Selective Cathepsin Inhibitors" @default.
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• W2044280138 doi "https://doi.org/10.1021/jm101272p" @default.
• W2044280138 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21128614" @default.
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