Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/35327
metadata.artigo.dc.title: The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study
metadata.artigo.dc.creator: Cuya, Teobaldo
Gonçalves, Arlan da Silva
Silva, Jorge Alberto Valle da
Ramalho, Teodorico C.
Kuca, Kamil
França, Tanos C.C.
metadata.artigo.dc.subject: HI-6
HS-6
Acetylcholinesterase
Molecular modeling
Chemical defense
Oximes
metadata.artigo.dc.publisher: Taylor & Francis
metadata.artigo.dc.date.issued: 2018
metadata.artigo.dc.identifier.citation: 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.
metadata.artigo.dc.description.abstract: 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.
metadata.artigo.dc.identifier.uri: https://www.tandfonline.com/doi/full/10.1080/07391102.2017.1389307
http://repositorio.ufla.br/jspui/handle/1/35327
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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