Towards understanding the interaction of β-lactoglobulin with capsaicin: Multi-spectroscopic, thermodynamic, molecular docking and molecular dynamics simulation approaches
Towards understanding the interaction of β-lactoglobulin with capsaicin: Multi-spectroscopic, thermodynamic, molecular docking and molecular dynamics simulation approaches
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理解β-乳球蛋白与辣椒素的相互作用：多光谱、热力学、分子对接和分子动力学模拟方法
DOI：
10.1016/j.foodhyd.2020.105767
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发表时间：
2020-08-01
影响因子：
10.7
通讯作者：
Chen, Yijie
中科院分区：
文献类型：
--
作者：
Zhan, Fuchao;Ding, Shuang;Chen, Yijie
采用多光谱、热力学、分子对接和分子动力学模拟等方法，系统研究了pH 7.4条件下辣椒素（CAP）与β-乳球蛋白（β-lg）的结合机理。结果表明，CAP能与β-lg相互作用，增强β-lg的荧光强度，同时，CAP与β-lg形成的复合物增强了β-lg中色氨酸和酪氨酸微环境的疏水性。粒径的变化不改变β-lg的二级结构，表明β-lg的大聚集体颗粒向小聚集体颗粒转变。ITC）结果表明，疏水相互作用在复合物的形成中起着重要作用。MD仿真结果表明，在30 ns的仿真时间后，系统的RMSD达到平衡，并在平均值附近摆动。Rg分析表明β-lg和β-lg/CAP复合物在30 ns左右稳定。二级结构分析结果表明CAP对β-Ig结构没有明显影响。分子动力学模拟结果表明，β-lg与CAP的结合也存在货车范德华相互作用。计算结果表明，CAP优先结合在β-lg的疏水口袋中，这为β-lg与CAP的相互作用机理提供了新的线索，证明β-lg具有作为辣椒碱载体应用于功能食品的能力。
This study systematically investigated the binding mechanism between capsaicin (CAP) and beta-lactoglobulin (beta-lg) through the method of multi-spectroscopic, thermodynamics, molecular docking, and molecular dynamics simulation at pH 7.4. The results showed that CAP could interact with beta-lg to enhance the fluorescence intensity of beta-lg. Simultaneously, the complex formed by CAP and beta-lg enhanced the hydrophobicity of the microenvironment of Trp and Tyr in beta-lg. The change in particle size without changing the secondary structure of beta-lg indicates a transition between the large aggregate particle to small aggregate particle of beta-lg. Isothermal titration calorimetric (ITC) results show that hydrophobic interactions play an important role in the formation of the complex. The MD simulation results showed that the RMSD of the systems reached equilibrium and wiggle around the mean value after 30 ns of simulation time. Analysis of Rg indicated that beta-lg and beta-lg/CAP complex was stabilized around 30 ns. Secondary structure analysis results showed that CAP has no distinct effect on the beta-lg structure. Furthermore, the van der Waals interactions are also involved in binding between beta-lg and CAP according to the result of MD simulation. The calculational results indicated that CAP preferred to bind to the hydrophobic pocket of beta-lg. The obtained results could provide some new clues to the interaction mechanism of beta-lg and CAP, which proved that beta-lg possesses the ability to apply in functional food as the vehicle of capsaicin.