Novel oxoisoaporphine-based inhibitors of acetyl- and butyrylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation

Bioorg Med Chem Lett. 2012 Mar 15;22(6):2257-61. doi: 10.1016/j.bmcl.2012.01.090. Epub 2012 Jan 31.

Abstract

A series of novel oxoisoaporphine-based inhibitors (10-aminoalkylamino-1-azabenzanthrone Ar-NH(CH(2))(n)NR(1)R(2)) of acetylcholinesterase (AChE) has been designed, synthesized, and tested for their ability to inhibit AChE, butyrylcholinesterase (BChE) and AChE-induced β-amyloid (Aβ) aggregation. The synthetic compounds exhibited high AChE inhibitory activity with IC(50) values in the submicromolar range in most cases. Non-competitive binding mode was found for these derivatives by the graphical analysis of steady-state inhibition data. Moreover, all compounds exhibit significant inhibitory activity on AChE-induced Aβ aggregation with inhibitory potency from 54.5% to 93.5%. Finally, six out of twelve synthetic compounds were predicted to be able to cross the blood-brain barrier (BBB) to reach their targets in the central nervous system (CNS) according to a parallel artificial membrane permeation assay for BBB. The result encourages us to study this class of compounds thoroughly and systematically.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / metabolism*
  • Alzheimer Disease / drug therapy
  • Alzheimer Disease / enzymology
  • Amyloid beta-Peptides / antagonists & inhibitors*
  • Aporphines / chemical synthesis*
  • Aporphines / pharmacology
  • Binding Sites
  • Blood-Brain Barrier / metabolism
  • Butyrylcholinesterase / metabolism*
  • Cholinesterase Inhibitors / chemical synthesis*
  • Cholinesterase Inhibitors / pharmacology
  • Humans
  • Membranes, Artificial
  • Models, Molecular
  • Molecular Structure
  • Permeability
  • Protein Binding

Substances

  • Amyloid beta-Peptides
  • Aporphines
  • Cholinesterase Inhibitors
  • Membranes, Artificial
  • Acetylcholinesterase
  • Butyrylcholinesterase