Reactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study

dc.creatorSilva, Jorge Alberto Valle da
dc.creatorPereira, Ander Francisco
dc.creatorLaPlante, Steven R.
dc.creatorKuca, Kamil
dc.creatorRamalho, Teodorico Castro
dc.creatorFrança, Tanos Celmar Costa
dc.date2020-09-10T13:58:59Z
dc.date2020-09-10T13:58:59Z
dc.date2020
dc.date.accessioned2023-09-28T20:08:11Z
dc.date.available2023-09-28T20:08:11Z
dc.identifierSILVA, J. A. V. da et al. Reactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study. Biomolecules, [S.l.], v. 10, n. 2, 2020.
dc.identifierhttps://www.mdpi.com/2218-273X/10/2/192/htm
dc.identifierhttp://repositorio.ufla.br/jspui/handle/1/42973
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/9045314
dc.descriptionIn the present work, we performed a complementary quantum mechanical (QM) study to describe the mechanism by which deprotonated pralidoxime (2-PAM) could reactivate human (Homo sapiens sapiens) acetylcholinesterase (HssAChE) inhibited by the nerve agent VX. Such a reaction is proposed to occur in subsequent addition–elimination steps, starting with a nucleophile bimolecular substitution (SN2) mechanism through the formation of a trigonal bipyramidal transition state (TS). A near attack conformation (NAC), obtained in a former study using molecular mechanics (MM) calculations, was taken as a starting point for this project, where we described the possible formation of the TS. Together, this combined QM/MM study on AChE reactivation shows the feasibility of the reactivation occurring via attack of the deprotonated form of 2-PAM against the Ser203-VX adduct of HssAChE.
dc.languageen_US
dc.publisherMultidisciplinary Digital Publishing Institute
dc.rightsrestrictAccess
dc.sourceBiomolecules
dc.subjectAcetylcholinesterase
dc.subjectPralidoxime (2-PAM)
dc.subjectQuantum Mechanics/Molecular Mechanics method (QM/MM)
dc.titleReactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study
dc.typeArtigo


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