Arylaminoethyl amides as novel non-covalent cathepsin K inhibitors

J Med Chem. 2002 Jun 6;45(12):2352-4. doi: 10.1021/jm010801s.

Abstract

A series of N(alpha)-benzyloxycarbonyl- and N(alpha)-acyl-L-leucine(2-phenylaminoethyl)amide derivatives were prepared and evaluated for their inhibitory activity against rabbit and human cysteine proteases cathepsins K, L, and S. These data indicate that N(alpha)-acyl-alpha-amino acid-(arylaminoethyl)amides represent a new class of selective non-covalent inhibitors of cathepsin K. Compounds 4b, 4e, and 4g exhibit high potency toward rabbit and human cathepsin K (IC(50) < 0.006 microM) and are characterized by an excellent selectivity profile vs human cathepsins L and S.

MeSH terms

  • Amides / chemical synthesis*
  • Amides / chemistry
  • Animals
  • Cathepsin K
  • Cathepsins / antagonists & inhibitors*
  • Cathepsins / chemistry
  • Cysteine Proteinase Inhibitors / chemical synthesis*
  • Cysteine Proteinase Inhibitors / chemistry
  • Fluorescence
  • Humans
  • Kinetics
  • Rabbits
  • Recombinant Proteins / antagonists & inhibitors
  • Recombinant Proteins / chemistry
  • Structure-Activity Relationship

Substances

  • Amides
  • Cysteine Proteinase Inhibitors
  • Recombinant Proteins
  • Cathepsins
  • CTSK protein, human
  • Cathepsin K