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

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorSilva, Jorge Alberto Valle da-
Autor(es): dc.creatorPereira, Ander Francisco-
Autor(es): dc.creatorLaPlante, Steven R.-
Autor(es): dc.creatorKuca, Kamil-
Autor(es): dc.creatorRamalho, Teodorico Castro-
Autor(es): dc.creatorFrança, Tanos Celmar Costa-
Data de aceite: dc.date.accessioned2026-02-09T11:23:44Z-
Data de disponibilização: dc.date.available2026-02-09T11:23:44Z-
Data de envio: dc.date.issued2020-09-10-
Data de envio: dc.date.issued2020-09-10-
Data de envio: dc.date.issued2019-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/42973-
Fonte completa do material: dc.identifierhttps://www.mdpi.com/2218-273X/10/2/192/htm-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1139953-
Descrição: 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.-
Idioma: dc.languageen-
Publicador: dc.publisherMultidisciplinary Digital Publishing Institute-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceBiomolecules-
Palavras-chave: dc.subjectAcetylcholinesterase-
Palavras-chave: dc.subjectPralidoxime (2-PAM)-
Palavras-chave: dc.subjectQuantum Mechanics/Molecular Mechanics method (QM/MM)-
Título: dc.titleReactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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