Alpha-glucosidase inhibitors with a phthalimide skeleton: structure-activity relationship study

Chem Pharm Bull (Tokyo). 2000 Oct;48(10):1494-9. doi: 10.1248/cpb.48.1494.

Abstract

Alpha-glucosidase inhibitors with a phthalimide skeleton were prepared. Structure-activity relationship studies indicated a critical role for the hydrophobicity of the substituent at the nitrogen atom of the phthalimide skeleton. Introduction of electron-withdrawing groups, including a nitro group and chlorine, influenced the activity. Optimization studies led us to design 4,5,6,7-tetrachloro-N-phenylphthalimide (CPOP) and its N-phenylalkyl derivatives. CP0P and 4,5,6,7-tetrachloro-N-(4-phenylbutyl)phthalimide (CP4P) proved to be more potent alpha-glucosidase inhibitors than the known inhibitor 1-deoxynojirimycin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkylation
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Glycoside Hydrolase Inhibitors*
  • Magnetic Resonance Spectroscopy
  • Phthalimides / chemistry*
  • Structure-Activity Relationship

Substances

  • Enzyme Inhibitors
  • Glycoside Hydrolase Inhibitors
  • Phthalimides