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|metadata.artigo.dc.title:||Reactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study|
|metadata.artigo.dc.creator:||Silva, Jorge Alberto Valle da|
Pereira, Ander Francisco
LaPlante, Steven R.
Ramalho, Teodorico Castro
França, Tanos Celmar Costa
Quantum Mechanics/Molecular Mechanics method (QM/MM)
|metadata.artigo.dc.publisher:||Multidisciplinary Digital Publishing Institute|
|metadata.artigo.dc.identifier.citation:||SILVA, J. A. V. da et al. Reactivation of VX-inhibited human acetylcholinesterase by deprotonated pralidoxime. a complementary quantum mechanical study. Biomolecules, [S.l.], v. 10, n. 2, 2020.|
|metadata.artigo.dc.description.abstract:||In 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.|
|Appears in Collections:||DQI - Artigos publicados em periódicos|
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