Characterization the non-covalent interactions between beta lactoglobulin and selected phenolic acids
Characterization the non-covalent interactions between beta lactoglobulin and selected phenolic acids
复制标题
表征 β 乳球蛋白和选定酚酸之间的非共价相互作用
DOI：
10.1016/j.foodhyd.2020.105761
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发表时间：
2020-08-01
影响因子：
10.7
通讯作者：
Li, Ti
中科院分区：
文献类型：
--
作者：
Li, Xin;Dai, Taotao;Li, Ti
采用光谱法和分子对接技术研究了β-乳球蛋白（β-LG）与3，4-二羟基苯甲酸、没食子酸、胡萝卜酸、咖啡酸、阿魏酸和绿原酸等酚酸的相互作用。荧光猝灭表明形成了稳定的酚酸-β-LG复合物。热力学参数表明，疏水力主导了相互作用过程，并通过分子对接研究了相互作用。圆二色谱显示所选酚酸诱导β-LG的二级结构从β-折叠转变为β-转角和α-螺旋。两种酚酸对β-LG的表面疏水性有不同的影响，其结合亲和力的大小顺序为CaA > ChA > FA > SA > DA > GA，说明羟基化、甲基化、空间位阻和酚酸的种类对β-LG的结合亲和力有影响。肉桂酸衍生物（CaA、FA和ChA）比苯甲酸衍生物（DA、GA和SA）表现出更强的与β-LG的结合亲和力。甲基化和羟基数目对酚酸的影响取决于酚酸的类型，空间位阻效应降低了它们的结合能力。本文的研究结果有助于揭示酚酸与β-乳球蛋白的结合机制。
The interactions between beta-lactoglobulin (beta-LG) and two types of phenolic acids, including 3,4-dihydroxybenzoic acid, gallic acid, syringic acid, caffeic acid, ferulic acid, and chlorogenic acid, were investigated by spectroscopy and molecular docking. The fluorescence quenching suggested the formation of a stable phenolic acid-beta-LG complex. The thermodynamic parameters suggested that hydrophobic forces dominated the interaction process and the interaction was studied by the molecular docking. The circular dichroism spectra showed the selected phenolic acid induced secondary structure transition of the beta-LG from beta-sheet to beta-turn and alpha-helix. Interestingly, two types of selected phenolic acids had different effects on the surface hydrophobicity of beta-LG. Furthermore, the binding affinity decreased in the order CaA > ChA > FA > SA > DA > GA, which revealed that hydroxylation, methylation, steric hindrance and the type of phenolic acids affected the binding affinity. Cinnamic acid derivatives (CaA, FA, and ChA) exhibited a stronger binding affinity with beta-LG than benzoic acid derivatives (DA, GA, and SA). The influence of methylation and the number of hydroxyl groups on the phenolic acids depended on phenolic acid type, the steric hindrance effects reduced their binding ability. The findings obtained herein are helpful to bring out the binding mechanism of phenolic acids and beta-lactoglobulin.