β-乳球蛋白与阿魏酸分子相互作用的pH依赖性的光谱和分子对接联合研究,Food Hydrocolloids

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β-乳球蛋白与阿魏酸分子相互作用的pH依赖性的光谱和分子对接联合研究
Food Hydrocolloids ( IF 11.0 ) Pub Date : 2020-04-01 , DOI: 10.1016/j.foodhyd.2019.105461
Kourosh Abdollahi , Cameron Ince , Lloyd Condict , Andrew Hung , Stefan Kasapis

摘要在环境温度下研究了 β-乳球蛋白和阿魏酸之间的相互作用，分别与 pH 7.3 和 2.4 下蛋白质的二聚体和单体形式有关。为此，采用了分子动力学 (MD) 模拟和各种光谱方法。圆二色性 (CD) 和傅里叶变换红外 (FTIR) 分析表明，复合后蛋白质的二级结构发生了改变，表明分子相互作用确实以单体和二聚体形式发生。然而，β-乳球蛋白的 UV-vis 测量在与阿魏酸络合后保持恒定，表明相互作用本质上是非共价的，并且可能通过疏水力和氢键稳定。荧光猝灭证实了结合状态的存在，单体复合物产生比二聚体对应物更强的解离常数。对接研究和 MD 模拟表明，二聚体形式 (pH 7.3) 的首选结合位点位于两种单体的界面处。相比之下，单体形式 (pH 2.4) 的优选结合位点位于花萼形 β-桶结构内，并通过氢键和 π-烷基相互作用稳定。

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Combined spectroscopic and molecular docking study on the pH dependence of molecular interactions between β-lactoglobulin and ferulic acid

Abstract Interactions between β-lactoglobulin and ferulic acid were investigated at ambient temperature in relation to the dimer and monomer forms of the protein at pH 7.3 and 2.4, respectively. To this end, molecular dynamics (MD) simulations and a variety of spectroscopic methods were employed. Circular dichroism (CD) and Fourier transform infrared (FTIR) analysis indicate that the secondary structure of the protein is altered upon complexation, suggesting molecular interactions do occur in both the monomer and dimer forms. However, UV–vis measurements of β-lactoglobulin remain constant upon complexation with ferulic acid, indicating that interactions are non-covalent in nature and are likely stabilised by hydrophobic forces and hydrogen bonds. Fluorescence quenching confirms the presence of a binding state, with the monomeric complex producing a stronger dissociation constant than the dimeric counterpart. Docking studies and MD simulations indicate that the preferred binding site in the dimer form (pH 7.3) lies at the interface of the two monomers. In contrast, the preferred binding site for the monomer form (pH 2.4) lies within the calyx shaped β-barrel structure and is stabilised by hydrogen bonds and π - alkyl interactions.

更新日期：2020-04-01

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