The design and optimization of a series of 2-(pyridin-2-yl)-1H-benzimidazole compounds as allosteric glucokinase activators

Bioorg Med Chem. 2009 Oct 1;17(19):7042-51. doi: 10.1016/j.bmc.2009.05.037. Epub 2009 May 21.

Abstract

The optimization of a series of benzimidazole glucokinase activators is described. We identified a novel and potent achiral benzimidazole derivative as an allosteric GK activator. This activator was designed and synthesized via removal of the chiral center of the lead compound, 6-(N-acylpyrrolidin-2-yl)benzimidazole. The activator exhibited good PK profiles in rats and dogs, and significant hypoglycemic efficacy at 1 mg/kg po dosing in a rat OGTT model. The binding site and binding mode of the benzimidazole class of GKA with GK protein was confirmed by X-ray crystallographic analysis.

MeSH terms

  • Allosteric Regulation / drug effects
  • Animals
  • Benzimidazoles / chemical synthesis*
  • Benzimidazoles / pharmacology
  • Binding Sites
  • Crystallography, X-Ray
  • Dogs
  • Drug Design
  • Glucokinase / drug effects*
  • Hypoglycemic Agents / chemical synthesis
  • Rats

Substances

  • Benzimidazoles
  • Hypoglycemic Agents
  • Glucokinase

Associated data

  • PDB/3H1V