Design and synthesis of conformationally-constrained MMP inhibitors

Bioorg Med Chem Lett. 1998 Aug 18;8(16):2077-80. doi: 10.1016/s0960-894x(98)00370-9.

Abstract

A novel series of conformationally constrained matrix metalloprotease inhibitors was identified. The potencies observed for these inhibitors were highly dependent upon the substitution pattern on the caprolactam ring as well as the succinate moiety.

MeSH terms

  • Caprolactam / analogs & derivatives*
  • Caprolactam / chemical synthesis*
  • Caprolactam / chemistry
  • Caprolactam / pharmacology
  • Collagenases / chemistry
  • Drug Design
  • Indicators and Reagents
  • Kinetics
  • Matrix Metalloproteinase 1
  • Matrix Metalloproteinase 3 / chemistry
  • Matrix Metalloproteinase Inhibitors
  • Metalloendopeptidases / antagonists & inhibitors*
  • Models, Molecular
  • Molecular Conformation
  • Molecular Structure
  • Protease Inhibitors / chemical synthesis*
  • Protease Inhibitors / chemistry*
  • Protease Inhibitors / pharmacology
  • Protein Conformation
  • Structure-Activity Relationship
  • Succinates / chemical synthesis
  • Succinates / chemistry
  • Succinates / pharmacology

Substances

  • Indicators and Reagents
  • Matrix Metalloproteinase Inhibitors
  • Protease Inhibitors
  • Succinates
  • Caprolactam
  • Collagenases
  • Metalloendopeptidases
  • Matrix Metalloproteinase 3
  • Matrix Metalloproteinase 1