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首页> 外文期刊>Journal of the Brazilian Chemical Society >Molecular dynamics of the interaction of pralidoxime and deazapralidoxime with acetylcholinesterase inhibited by the neurotoxic agent tabun
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Molecular dynamics of the interaction of pralidoxime and deazapralidoxime with acetylcholinesterase inhibited by the neurotoxic agent tabun

机译：神经毒性剂塔博恩抑制普利扑肟和脱氮杂ral肟与乙酰胆碱酯酶相互作用的分子动力学

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摘要

Efficient acetylcholinesterase reactivators are fundamental for the development of antidotes against poisoning by neurotoxic pesticides and chemical warfare agents. However, the mechanism of the reactivation reaction and the structural characteristics of the known reactivators are poorly understood. In order to study the dynamic behavior and the effect of the antidote net charge in the reactivation of this enzyme, we carried out a molecular dynamics study of human acetylcholinesterase inhibited by tabun in complex with the antidote pralidoxime and with its deaza analogues in the neutral and anionic forms. Results show that the positive charge of pralidoxime is important for its admission and permanence inside the active site. Also, the analogues, unlike pralidoxime, when forced inside the active site, move away from the phosphorilated serine residue of the enzyme and are repelled by the electrostatic potential at the entrance of the channel that conducts to the active site.
机译：高效的乙酰胆碱酯酶活化剂对于开发针对神经毒性农药和化学战剂中毒的解毒剂至关重要。然而，对再活化反应的机理和已知再活化剂的结构特征了解得很少。为了研究解毒剂净电荷在该酶的再活化中的动力学行为和作用，我们进行了分子动力学研究，研究了塔宾对人乙酰胆碱酯酶的抑制作用，该酶与解毒剂普利多肟及其deaza类似物在中性和酸性条件下复合。阴离子形式。结果表明，普利多肟的正电荷对其在活性部位的接纳和持久性很重要。同样，与普利昔肟不同，类似物在被迫进入活性位点后，会从酶的磷酸丝氨酸残基移开，并被传导至活性位点的通道入口处的静电势所排斥。

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