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

Akinori Hirashima; Eiichi Kuwano; Morifusa Eto

doi:10.1016/S0968-0896(99)00315-6

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

Akinori Hirashima, Eiichi Kuwano, Morifusa Eto

Molecular Biosciences

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	653-656
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry
Volume	8
Issue number	3
DOIs	https://doi.org/10.1016/S0968-0896(99)00315-6
Publication status	Published - Mar 2000

All Science Journal Classification (ASJC) codes

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

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10.1016/S0968-0896(99)00315-6

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title = "Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase",

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.",

author = "Akinori Hirashima and Eiichi Kuwano and Morifusa Eto",

note = "Funding Information: This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.",

year = "2000",

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T1 - Docking study of enantiomeric fonofos oxon bound to the active site of Torpedo californica acetylcholinesterase

AU - Hirashima, Akinori

AU - Kuwano, Eiichi

AU - Eto, Morifusa

N1 - Funding Information: This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.

PY - 2000/3

Y1 - 2000/3

N2 - 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.

AB - 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.

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JO - Bioorganic and Medicinal Chemistry

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

Abstract

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