Use este identificador para citar ou linkar para este item: http://repositorio.ufla.br/jspui/handle/1/35327
Título: The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study
Palavras-chave: HI-6
HS-6
Acetylcholinesterase
Molecular modeling
Chemical defense
Oximes
Data do documento: 2018
Editor: Taylor & Francis
Citação: CUYA, T. et al. The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study. Journal of Biomolecular Structure and Dynamics, [S.l.], v. 36, n. 13, p. 3444-3452, 2018. DOI: 10.1080/07391102.2017.1389307.
Resumo: The oximes 4-carbamoyl-1-[({2-[(E)-(hydroxyimino) methyl] pyridinium-1-yl} methoxy) methyl] pyridinium (known as HI-6) and 3-carbamoyl-1-[({2-[(E)-(hydroxyimino) methyl] pyridinium-1-yl} methoxy) methyl] pyridinium (known as HS-6) are isomers differing from each other only by the position of the carbamoyl group on the pyridine ring. However, this slight difference was verified to be responsible for big differences in the percentual of reactivation of acetylcholinesterase (AChE) inhibited by the nerve agents tabun, sarin, cyclosarin, and VX. In order to try to find out the reason for this, a computational study involving molecular docking, molecular dynamics, and binding energies calculations, was performed on the binding modes of HI-6 and HS-6 on human AChE (HssAChE) inhibited by those nerve agents.
URI: https://www.tandfonline.com/doi/full/10.1080/07391102.2017.1389307
http://repositorio.ufla.br/jspui/handle/1/35327
Aparece nas coleções:DQI - Artigos publicados em periódicos

Arquivos associados a este item:
Não existem arquivos associados a este item.


Os itens no repositório estão protegidos por copyright, com todos os direitos reservados, salvo quando é indicado o contrário.