Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/35327
Title: The role of the oximes HI-6 and HS-6 inside human acetylcholinesterase inhibited with nerve agents: a computational study
Keywords: HI-6
HS-6
Acetylcholinesterase
Molecular modeling
Chemical defense
Oximes
Issue Date: 2018
Publisher: Taylor & Francis
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.
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.
URI: https://www.tandfonline.com/doi/full/10.1080/07391102.2017.1389307
http://repositorio.ufla.br/jspui/handle/1/35327
Appears in Collections:DQI - Artigos publicados em periódicos

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.