Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 55, Issue 12, Pages 5982-5986Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm300734k
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Funding
- NRW International Research School Biotech-Pharma
- German Research Foundation [GRK 804]
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A series of dipeptide nitriles with different P3 substituents was designed to explore the S3 binding pocket of cathepsin S. Racemic 7-16 and the enantiopure derivative (R)-22 proved to be potent inhibitors of human cathepsin S and exhibited notable selectivity over human cathepsins L, K, and B. Inhibition of cathepsin F, the functional synergist of cathepsin S, was not observed. The azadipeptide analogue of 22, compound 26, was highly potent but nonselective.
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