Docking and quantum mechanic studies on cholinesterases and their inhibitors

José Correa-Basurto, Cesar Flores-Sandoval, Jesús Marín-Cruz, Arturo Rojo-Domínguez, L. Michel Espinoza-Fonseca, José G. Trujillo-Ferrara

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58 Scopus citations


Docking studies and density functional theory (DFT) calculations were made for 88 N-aryl derivatives and for some acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) residues. Based on this information, some compounds were synthesized and tested kinetically in vitro as AChE inhibitors. Finally, some chemical properties of the N-aryl derivatives were calculated: partition coefficient (π) and molecular electrostatic potentials (MESPs) whereas their electronic effects (ρ) were taken from the literature. The results showed that all compounds act inside the AChE gorge, making π-π interactions and hydrogen bonds with Trp86 and Ser203 and by high HOMO energies of Ser2003 and high LUMO energies of N-aryl derivatives. These theoretical calculations for AChE are in agreement with the experimental data, whereas such calculations for BChE do not show the same behavior which could be due to in spite of both cholinesterase enzymes displaying similar functional activities they do possess important structural differences at their catalystic sites.

Original languageEnglish (US)
Pages (from-to)10-19
Number of pages10
JournalEuropean Journal of Medicinal Chemistry
Issue number1
StatePublished - Jan 2007
Externally publishedYes

Bibliographical note

Funding Information:
We are grateful to CONACyT (46168-M and ECOS M05-S01), COFAA-SIP/IPN and Programa de Ingeniería Molecular del IMP for scholarships and financial support to the authors.

Copyright 2008 Elsevier B.V., All rights reserved.


  • Acetylcholinesterase
  • Alzheimer's disease
  • Butyrylcholinesterase
  • Docking
  • HOMO-LUMO densities
  • N-aryl derivatives


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