The Gabriel-Colman rearrangement in biological systems: design, synthesis and biological evaluation of phthalimide and saccharin derivatives as potential mechanism-based inhibitors of human leukocyte elastase, cathepsin G and proteinase 3

Bioorg Med Chem. 1995 Feb;3(2):187-93. doi: 10.1016/0968-0896(95)00013-7.

Abstract

The results of a structure-activity relationship study focusing on the interaction of a series of phthalimide and saccharin derivatives with leukocyte elastase, cathepsin G and proteinase 3 are described. The phthalimide derivatives were found to be inactive while some of the saccharin derivatives were found to be fair inhibitors of these enzymes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cathepsin G
  • Cathepsins / antagonists & inhibitors*
  • Humans
  • Leukocyte Elastase
  • Magnetic Resonance Spectroscopy
  • Myeloblastin
  • Pancreatic Elastase / antagonists & inhibitors*
  • Phthalimides / chemical synthesis*
  • Phthalimides / chemistry
  • Phthalimides / pharmacology
  • Saccharin / analogs & derivatives*
  • Saccharin / chemical synthesis
  • Saccharin / chemistry
  • Saccharin / pharmacology
  • Serine Endopeptidases / drug effects*
  • Structure-Activity Relationship

Substances

  • Phthalimides
  • Cathepsins
  • Serine Endopeptidases
  • CTSG protein, human
  • Cathepsin G
  • Pancreatic Elastase
  • Leukocyte Elastase
  • Myeloblastin
  • Saccharin