Computational Evidence for the Reactivation Process of Human Acetylcholinesterase Inhibited by Carbamates

Author(s): Karina Silvia Matos, Elaine F. F. da Cunha, Ruben Abagyan, Teodorico C. Ramalho

Journal Name: Combinatorial Chemistry & High Throughput Screening
Accelerated Technologies for Biotechnology, Bioassays, Medicinal Chemistry and Natural Products Research

Volume 17 , Issue 6 , 2014

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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.

Keywords: Acetylcholinesterase, Docking studies, Neurotoxic agents, Oximes, theoretical calculation.

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Article Details

Year: 2014
Published on: 26 June, 2014
Page: [554 - 564]
Pages: 11
DOI: 10.2174/1386207316666131217100416
Price: $65

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