Majumdar D, Roszak Szczepan, Leszczynski Jerzy
Computational Center for Molecular Structure and Interactions, Department of Chemistry, Jackson State University, Jackson, Mississippi 39217, USA.
J Phys Chem B. 2006 Jul 13;110(27):13597-607. doi: 10.1021/jp061497n.
Interaction energies have been estimated between sarin and a model enzyme cavity of acetylcholinesterase (ACHE) using the density functional and Møller-Plesset second-order perturbation (MP2) levels of theories. The calculated interaction energies have been compared with those of acetylcholine and the same model ACHE cavity. The ACHE...sarin and ACHE...acetylcholine (Ach) structures have been optimized using DFT based two-layer ONIOM hybrid calculations. The nature of interactions has been investigated in detail using an interaction energy partitioning technique. The effects of solvation on the interaction energies have also been taken into account. An inhibition mechanism during the uptake of sarin inside the ACHE cavity has been proposed from the comparison of the energetics of the ACHE...sarin and ACHE...Ach complexes.
利用密度泛函理论和莫勒-普莱塞特二阶微扰（MP2）理论水平，估算了沙林与乙酰胆碱酯酶（ACHE）模型酶腔之间的相互作用能。已将计算得到的相互作用能与乙酰胆碱和相同ACHE模型腔的相互作用能进行了比较。ACHE……沙林和ACHE……乙酰胆碱（Ach）结构已使用基于密度泛函理论（DFT）的两层ONIOM混合计算进行了优化。已使用相互作用能划分技术详细研究了相互作用的性质。还考虑了溶剂化对相互作用能的影响。通过比较ACHE……沙林和ACHE……Ach复合物的能量学，提出了沙林在ACHE腔内摄取过程中的抑制机制。
