Extensive SAR and computational studies of 3-{4-[(benzylmethylamino)methyl]phenyl}-6,7-dimethoxy-2H-2-chromenone (AP2238) derivatives

J Med Chem. 2007 Aug 23;50(17):4250-4. doi: 10.1021/jm070100g. Epub 2007 Jul 26.

Abstract

AP2238 was the first compound published to bind both anionic sites of the human acetylcholinesterase, allowing the simultaneous inhibition of the catalytic and the amyloid-beta pro-aggregating activities of AChE. Here we attempted to derive a comprehensive structure-activity relationship picture for this molecule, affording 28 derivatives for which AChE and BChE inhibitory activities were evaluated. Selected compounds were also tested for their ability to prevent the AChE-induced Abeta-aggregation. Moreover, docking simulations and molecular orbital calculations were performed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / chemistry
  • Benzylamines / chemical synthesis*
  • Benzylamines / chemistry
  • Butyrylcholinesterase / chemistry
  • Catalytic Domain
  • Cholinesterase Inhibitors / chemical synthesis*
  • Cholinesterase Inhibitors / chemistry
  • Computer Simulation*
  • Coumarins / chemical synthesis*
  • Coumarins / chemistry
  • Humans
  • Models, Molecular*
  • Quantum Theory
  • Structure-Activity Relationship

Substances

  • AP 2238
  • Benzylamines
  • Cholinesterase Inhibitors
  • Coumarins
  • Acetylcholinesterase
  • Butyrylcholinesterase