Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase

Akinori Hirashima, Eiichi Kuwano, Morifusa Eto

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

Molecular interaction between enantiomeric fonofos oxon (O-ethyl S-phenyl ethylphosphonothiolate) and acetylcholinesterase (AChE) of Torpedo californica was evaluated by using the Cerius2 program. It was suggested that the difference in the inhibitory activity of the two enantiomers of fonofos oxon on AChE is due to the steric hindrance in binding to the AChE active site. Copyright (C) 2000 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)653-656
Number of pages4
JournalBioorganic and Medicinal Chemistry
Volume8
Issue number3
DOIs
Publication statusPublished - Mar 2000

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase'. Together they form a unique fingerprint.

Cite this