Docking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorGuimarães, Ana Paula-
Autor(es): dc.creatorFrança, Tanos Celmar Costa-
Autor(es): dc.creatorRamalho, Teodorico Castro-
Autor(es): dc.creatorRennó, Magdalena Nascimento-
Autor(es): dc.creatorMatos, Karina Silvia-
Autor(es): dc.creatorMancini, Daiana Teixeira-
Autor(es): dc.creatorKuča, Kamil-
Data de aceite: dc.date.accessioned2026-02-09T12:17:29Z-
Data de disponibilização: dc.date.available2026-02-09T12:17:29Z-
Data de envio: dc.date.issued2018-01-26-
Data de envio: dc.date.issued2018-01-26-
Data de envio: dc.date.issued2011-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/28473-
Fonte completa do material: dc.identifierhttps://www.sciencedirect.com/science/article/pii/S1214021X14600363#!-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1158339-
Descrição: dc.descriptionIn order to contribute to a better understanding of the mechanism of action of oximes, we evaluated the affinities of 10 new oximes, derived from pyridine-imidazol bicycled systems, for human acetylcholinesterase (HssAChE) complexed with tabun, by estimating their docking energy values and comparing of the values obtained to known oximes using the software Molegro Virtual Docker (MVD)® We evaluated the influence of the position of the oxime group as substituent in the structures and, also, the influence of the oxime group syn-anti isomery on the docking score values for all the molecules studied. Results suggest that: the affinities of the 10 new oximes for the tabun inhibited HssAChE active site are better than pralidoxime's and similar to trimedoxime's; the meta-pralidoxime could have more affinity for the HssAChE active site and the oximes’ anti isomers could present slightly better affinities for the HssAChE active site than the syn isomers.-
Idioma: dc.languageen-
Publicador: dc.publisherElsevier-
Direitos: dc.rightsrestrictAccess-
???dc.source???: dc.sourceJournal of Applied Biomedicine-
Palavras-chave: dc.subjectAcetylcholinesterase-
Palavras-chave: dc.subjectDocking studies-
Palavras-chave: dc.subjectOximes-
Palavras-chave: dc.subjectNeurotoxic agents-
Palavras-chave: dc.subjectTheoretical calculation-
Palavras-chave: dc.subjectAcetilcolinesterase-
Palavras-chave: dc.subjectEstudos de docagem-
Palavras-chave: dc.subjectOximas-
Palavras-chave: dc.subjectAgentes neurotóxicos-
Palavras-chave: dc.subjectCálculo teórico-
Título: dc.titleDocking studies and effects of syn-anti isomery of oximes derived from pyridine imidazol bicycled systems as potential human acetylcholinesterase reactivators-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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