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首页> 外文期刊>Japanese Journal of Applied Physics. Part 2, Letters & Express Letters >Estimation of Ligand-Receptor Binding Affinity from Fluctuation of Their Interface
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Estimation of Ligand-Receptor Binding Affinity from Fluctuation of Their Interface

机译：从其界面的波动估计配体-受体的结合亲和力

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摘要

It is necessary for the understanding of protein interactions or in silico drug designs to accurately estimate ligand-receptor affinity. The energy calculation based on the electrostatic force, van der Waals force, and solvation effect is a direct method of computing the magnitude of the interaction between ligand and receptor. By this conventional method, however, it is difficult to estimate a slight difference in binding affinity with sufficient accuracy. We propose a novel concept for the evaluation of binding affinity between a ligand and its receptor by functionalizing the fluctuation at the ligand-receptor interface. This method enables an adequate estimation with a high accuracy compared with the conventional energetic approach. Human immunodeficiency virus type 1 (HIV-1) protease and its inhibitor are used to explain how binding affinity is extracted from the fluctuation in interfacial energy, and a combination of an antigen and its antibody is examined to demonstrate the compatibility between the estimation from the interfacial fluctuation and the experimentally measured binding energy.
机译：为了理解蛋白质相互作用或计算机药物设计，必须准确估计配体-受体亲和力。基于静电力，范德华力和溶剂化效应的能量计算是一种计算配体与受体相互作用程度的直接方法。然而，通过这种常规方法，难以以足够的精度估计结合亲和力的细微差异。我们提出了一种新的概念，通过功能化配体-受体界面的波动来评估配体与其受体之间的结合亲和力。与常规的能量方法相比，该方法能够以高精度进行适当的估计。人类免疫缺陷病毒1型（HIV-1）蛋白酶及其抑制剂用于解释如何从界面能的波动中提取结合亲和力，并检查抗原及其抗体的组合以证明两者之间的相容性。界面波动和实验测得的结合能。

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