Synthesis, biological evaluation and docking studies of novel bisquaternary aldoxime reactivators on acetylcholinesterase and butyrylcholinesterase inhibited by paraoxon

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MetadadosDescriçãoIdioma
Autor(es): dc.creatorKuca, Kamil-
Autor(es): dc.creatorJun, Daniel-
Autor(es): dc.creatorJunova, Lucie-
Autor(es): dc.creatorMusilek, Kamil-
Autor(es): dc.creatorHrabinova, Martina-
Autor(es): dc.creatorSilva, Jorge Alberto Valle da-
Autor(es): dc.creatorRamalho, Teodorico Castro-
Autor(es): dc.creatorValko, Marian-
Autor(es): dc.creatorWu, Qinghua-
Autor(es): dc.creatorNepovimova, Eugenie-
Autor(es): dc.creatorFrança, Tanos Celmar Costa-
Data de aceite: dc.date.accessioned2026-02-09T11:25:07Z-
Data de disponibilização: dc.date.available2026-02-09T11:25:07Z-
Data de envio: dc.date.issued2019-07-16-
Data de envio: dc.date.issued2019-07-16-
Data de envio: dc.date.issued2018-05-07-
Fonte completa do material: dc.identifierhttps://repositorio.ufla.br/handle/1/35326-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/1140388-
Descrição: dc.descriptionNerve agents and oxon forms of organophosphorus pesticides act as strong irreversible inhibitors of two cholinesterases in the human body: acetylcholinesterase (AChE; EC 3.1.1.7) and butyrylcholinesterase (BChE; EC 3.1.1.8), and are therefore highly toxic compounds. For the recovery of inhibited AChE, antidotes from the group of pyridinium or bispyridinium aldoxime reactivators (pralidoxime, obidoxime, HI-6) are used in combination with anticholinergics and anticonvulsives. Therapeutic efficacy of reactivators (called “oximes”) depends on their chemical structure and also the type of organophosphorus inhibitor. Three novel oximes (K131, K142, K153) with an oxime group in position four of the pyridinium ring were designed and then tested for their potency to reactivate human (Homo sapiens sapiens) AChE (HssACHE) and BChE (HssBChE) inhibited by the pesticide paraoxon (diethyl 4-nitrophenyl phosphate). According to the obtained results, none of the prepared oximes were able to satisfactorily reactivate paraoxon-inhibited cholinesterases. On the contrary, extraordinary activity of obidoxime in the case of paraoxon-inhibited HssAChE reactivation was confirmed. Additional docking studies pointed to possible explanations for these results.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Publicador: dc.publisherMolecular Diversity Preservation International (MDPI)-
Direitos: dc.rightsacesso aberto-
Direitos: dc.rightshttp://creativecommons.org/licenses/by/4.0/-
Direitos: dc.rightshttp://creativecommons.org/licenses/by/4.0/-
???dc.source???: dc.sourceMolecules-
Palavras-chave: dc.subjectAcetylcholinesterase-
Palavras-chave: dc.subjectAntidote-
Palavras-chave: dc.subjectButyrylcholinesterase-
Palavras-chave: dc.subjectOrganophosphate-
Palavras-chave: dc.subjectOxime-
Palavras-chave: dc.subjectParaoxon-
Título: dc.titleSynthesis, biological evaluation and docking studies of novel bisquaternary aldoxime reactivators on acetylcholinesterase and butyrylcholinesterase inhibited by paraoxon-
Tipo de arquivo: dc.typeArtigo-
Aparece nas coleções:Repositório Institucional da Universidade Federal de Lavras (RIUFLA)

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