Hurley Margaret M, Balboa Alex, Lushington Gerald H, Guo Jianxin
US Army Research Laboratory, APG, MD 21005-5066, USA.
Chem Biol Interact. 2005 Dec 15;157-158:321-5. doi: 10.1016/j.cbi.2005.10.096. Epub 2005 Nov 9.
Acetylcholinesterase (AChE) is an interesting research target not only because of its high enzyme catalytic rate but also because of the wide range of health effects resulting from its inhibition. This paper discusses results of a theoretical study of acetylcholinesterase inhibition using several simulation techniques. In the first technique, a novel method was developed and used for predicting the binding affinity of human AChE (huAChE) inhibitors. Results are also presented for classical molecular dynamics and quantum mechanical simulations. Theoretical proton NMR shift results are obtained and compared to experiment, and the importance of the Glu199 residue is discussed in the context of the model.
乙酰胆碱酯酶（AChE）是一个有趣的研究靶点，不仅因为其具有较高的酶催化速率，还因为抑制该酶会产生广泛的健康影响。本文讨论了使用几种模拟技术对乙酰胆碱酯酶抑制作用进行理论研究的结果。在第一种技术中，开发了一种新方法并用于预测人乙酰胆碱酯酶（huAChE）抑制剂的结合亲和力。还给出了经典分子动力学和量子力学模拟的结果。获得了理论质子核磁共振位移结果并与实验进行比较，并在模型背景下讨论了Glu199残基的重要性。
