基于多光谱和计算方法评价芥子酸及其 Cu(II)配合物与牛血清白蛋白的结合作用。
Multi-spectroscopic and computational evaluation on the binding of sinapic acid and its Cu(II) complex with bovine serum albumin.
机构信息
Department of Chemistry, Presidency University, 86/1 College Street, Kolkata 700073, India.
Chemical Sciences Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, Kolkata 700064, India.
出版信息
Food Chem. 2019 Dec 15;301:125254. doi: 10.1016/j.foodchem.2019.125254. Epub 2019 Jul 30.
Researches based on metal complexes of plant-derived phenolic acids have attracted much attention due to their beneficial applications in the development of functional food products, dietary supplements and pharmacology. Binding of phenolic acids with serum proteins greatly influences their pharmacological properties. In this context, interactions of a naturally occurring phenolic acid, sinapic acid (SA) and its Cu complex with a model transport protein, bovine serum albumin (BSA), have been explored by means of different spectroscopic and theoretical tools. Spectroscopic studies revealed that the interaction of SA and its Cu complex with BSA occurred through quenching of intrinsic fluorescence of BSA. Site-specific experimental and docking studies were performed to predict the binding site. The geometies of bound Cu and interacting residues of protein were predicted from a solution dynamics study. Interestingly, the complexation of SA with Cu enhanced the antioxidant activity of SA.
由于植物衍生的酚酸金属配合物在功能性食品产品、膳食补充剂和药理学的开发中有有益的应用，因此基于这些配合物的研究引起了广泛关注。酚酸与血清蛋白的结合极大地影响了它们的药理性质。在这种情况下，通过使用不同的光谱和理论工具，研究了一种天然存在的酚酸——芥子酸（SA）及其 Cu 配合物与模型转运蛋白牛血清白蛋白（BSA）的相互作用。光谱研究表明，SA 和其 Cu 配合物与 BSA 的相互作用是通过猝灭 BSA 的内源性荧光发生的。进行了基于实验和对接的位点特异性研究，以预测结合位点。从溶液动力学研究中预测了结合的 Cu 的几何形状和相互作用的蛋白质残基。有趣的是，SA 与 Cu 的络合增强了 SA 的抗氧化活性。
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