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metadata.artigo.dc.title: Computational evidence for the reactivation process of human acetylcholinesterase inhibited by carbamates
metadata.artigo.dc.creator: Matos, Karina Silva
Cunha, Elaine F. F. da
Abagyan, Ruben
Ramalho, Teodorico C.
metadata.artigo.dc.subject: Acetylcholinesterase
Docking studies
Neurotoxic agents
Estudos de docagem
Agentes neurotóxicos
metadata.artigo.dc.publisher: Bentham Science 2014
metadata.artigo.dc.identifier.citation: MATOS, K. S. et al. Computational evidence for the reactivation process of human acetylcholinesterase inhibited by carbamates. Combinatorial Chemistry & High Throughput Screening, [S. l.], v. 17, n. 6, p. 554-564, 2014.
metadata.artigo.dc.description.abstract: Acetylcholinesterase (AChE) is responsible for hydrolysis of acetylcholine (ACh), a function, which if disrupted, leads to cholinergic syndrome. Carbamates (CB) and organophosphorus compounds (OP) are AChE inhibitors, toxic and capable of causing severe poisoning or death to exposed individuals. The AChE reactivation is considered the main function of the oximes. In case of poisoning by CB, there is no consistent data in the literature for an oxime reactivation mechanism. In this work, we evaluated the affinity and reactivity of oximes with activity already reported against AChE inhibited by the OP chemical warfare agent ciclosarin, with MmAChE and HsAChE active sites inhibited by the CB pesticide carbofuran. Thus, our theoretical data indicate that HLO-7, BI-6 and K005 compounds may be promising reactivators of AChE inhibited by carbofuran.
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

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