Bioorganic & Medicinal Chemistry 2000-03-01

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

A Hirashima, E Kuwano, M Eto

文献索引：Bioorg. Med. Chem. 8(3) , 653-6, (2000)

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摘要

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.