The identification of potent, selective, and bioavailable cathepsin S inhibitors

Bioorg Med Chem Lett. 2007 Sep 1;17(17):4929-33. doi: 10.1016/j.bmcl.2007.06.023. Epub 2007 Jun 10.

Abstract

Highly potent, selective, and bioavailable inhibitors of human, mouse, or rat cathepsin S are described. The key structural features combine a sulfonyl moiety attached to a large group in P2 and a small substituent in P3.

MeSH terms

  • Animals
  • Cathepsins / antagonists & inhibitors*
  • Chemistry, Pharmaceutical / methods*
  • Cysteine Proteinase Inhibitors / chemistry
  • Drug Design
  • Drug Evaluation, Preclinical
  • Humans
  • Inhibitory Concentration 50
  • Mice
  • Models, Chemical
  • Models, Molecular
  • Molecular Conformation
  • Molecular Structure
  • Protein Binding
  • Rats
  • Structure-Activity Relationship

Substances

  • Cysteine Proteinase Inhibitors
  • Cathepsins
  • cathepsin S