Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors

J Med Chem. 2003 Jan 2;46(1):1-4. doi: 10.1021/jm0255668.

Abstract

Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.

MeSH terms

  • Acetylcholinesterase / chemistry*
  • Binding Sites
  • Butyrylcholinesterase / chemistry*
  • Cholinesterase Inhibitors / chemical synthesis*
  • Cholinesterase Inhibitors / chemistry
  • Drug Design
  • Ligands
  • Models, Molecular
  • Structure-Activity Relationship
  • Tacrine / chemical synthesis*
  • Tacrine / chemistry

Substances

  • Cholinesterase Inhibitors
  • Ligands
  • Tacrine
  • Acetylcholinesterase
  • Butyrylcholinesterase