Juan, Amor A. San Cho, Seung Joo 2024-01-21T02:30:31Z 2024-01-21T02:30:31Z 2022-01-10 2006-09-30 1738-642X https://pubs.kist.re.kr/handle/201004/135097 The cholinesterase-inhibiting organophosphorous (OP) compounds known as nerve agents are highly toxic. The principal toxic mechanism of OP compounds is the inhibition of acethylcholine esterase (AChE) by phosphorylation of its catalytic site. The reversible competitive inhibition of AChE may prevent the subsequent OP intoxication. In this study, three-dimensional quantitative structure-activity relationship (3D-QSAR) was performed to investigate the relationship between the 29 compounds with structural diversity and their bioactivities against AChE. In particular, predictive models were constructed using the comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA). The results indicate reasonable model for CoMFA (q(2) =0.453, r(2)= 0.697) and CoMSIA (q(2)= 0.518, r(2) = 0.696). The presence of steric and hydophobic group at naphtyl moiety of the model may lead to the design of improved competitive inhibitors for organophosphorous intoxication. English KOREAN SOC TOXICOGENOMICS & TOXICOPROTEOMICS NONQUATERNARY CHOLINESTERASE REACTIVATORS METHYLPHOSPHONYL-ACETYLCHOLINESTERASE INVITRO ETHYL METHYLPHOSPHONYL 3D-QSAR study of competitive inhibitor for acethylcholine esterase (AChE) nerve agent toxicity Article 1 MOLECULAR & CELLULAR TOXICOLOGY, v.2, no.3, pp.216 - 221 MOLECULAR & CELLULAR TOXICOLOGY 2 3 216 221 scie 000243596600010 Biochemistry & Molecular Biology Toxicology Biochemistry & Molecular Biology Toxicology Article NONQUATERNARY CHOLINESTERASE REACTIVATORS METHYLPHOSPHONYL-ACETYLCHOLINESTERASE INVITRO ETHYL METHYLPHOSPHONYL acethylcholine esterase competitive inhibitors CoMFA CoMSIA nerve agent