β-乳球蛋白与EGCG结合规律的分子动力学探究

doi:10.3969/j.issn.1673-1689.2022.01.007

首页 > 过刊浏览>2022年第41卷第1期 >51-59. DOI:10.3969/j.issn.1673-1689.2022.01.007

β-乳球蛋白与EGCG结合规律的分子动力学探究
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                        10.3969/j.issn.1673-1689.2022.01.007
                    
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Interaction between β--Lactoglobulin and Polyphenols Investigated by Molecular Dynamics Simulation

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为探究不同pH下多酚与蛋白质的结合规律，以茶多酚EGCG（表没食子儿茶素没食子酸酯）和β--乳球蛋白为研究对象，采用分子对接和分子模拟技术研究两者结合能、结合机制分别在pH为2、5、8时的变化。结果表明，EGCG主要结合在β--乳球蛋白的3个区域；在结合能最高的结合位点进行150 ns分子模拟过程中，发现EGCG的波动幅度比β-乳球蛋白大，特别是pH为2时，但EGCG的波动不会影响β-乳球蛋白结构的稳定；pH为5时β--乳球蛋白的疏水表面积、α-螺旋和β--折叠含量均为最低；EGCG与β--乳球蛋白在pH为5时结合能最高，pH为8时最低，pH为5时结合能最高主要由于此时疏水作用力、氢键和范德华力均最强。通过研究可知，pH会影响蛋白质表面结构，特别是蛋白质与小分子物质的结合处，从而影响两者间的结合能、结合位点和结合姿势。

Abstract:

For investigating the effects of pH on the binding between protein and polyphenols. The binding energy and binding mechanism between epigallocatechin gallate(EGCG) and β--lactoglobulin at pH 2, 5 and 8 were respectively studied using molecular docking and molecular dynamics simulation. EGCG mainly bound to 3 sites of β--lactoglobulin. The docking site with the highest binding energy was used for 150 ns molecular dynamics simulation. It was found that the fluctuation of small molecules was larger than that of protein, especially at pH 2, however, the fluctuation of small molecules did not affect the stability of protein structure. The hydrophobic surface area, the content of α-helix and β--sheet of protein were lowest at pH 5. The highest binding free energy of small molecules to protein was detected at pH 5, while the lowest at pH 8. The highest value was mainly due to the strongest hydrophobic force, hydrogen bond and van der Waals force at pH 5. The difference of pH would affect the surface structure of protein, especially the binding site, thus affecting the binding energy, binding site, and binding posture between protein and small molecule.

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孔庆新,黄业传,徐伟平,张径舟,刘碧林,李思阳.β-乳球蛋白与EGCG结合规律的分子动力学探究[J].食品与生物技术学报,2022,41(1):51-59.

KONG Qingxin, HUANG Yechuan, XU Weiping, ZHANG Jingzhou, LIU Bilin, LI Siyang. Interaction between β--Lactoglobulin and Polyphenols Investigated by Molecular Dynamics Simulation[J]. Journal of Food Science and Biotechnology,2022,41(1):51-59.

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在线发布日期: 2022-02-21
出版日期: 2022-01-25

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