Molecular spectroscopic studies on the interaction of morin with bovine serum albumin
Molecular spectroscopic studies on the interaction of morin with bovine serum albumin
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DOI：
10.1016/j.jphotobiol.2012.04.001
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发表时间：
2012-07-02
影响因子：
5.4
通讯作者：
Zhang, Li-Ping
中科院分区：
文献类型：
--
作者：
Hu, Yan-Jun;Yue, Hua-Li;Zhang, Li-Ping
在模拟生理条件下，采用分子光谱方法研究了不同温度下桑色素与牛血清白蛋白（BSA）的相互作用。随着桑色素浓度的增加，BSA的内源荧光猝灭是分析中的驱动工具。在不同温度下得到的猝灭机制、结合常数、结合位点和相应的热力学参数表明，疏水相互作用在桑色素-BSA缔合中起主要作用。利用Scatchard方程和改进的Stern-Volmer方程计算了桑色素与牛血清白蛋白的结合亲和力，并讨论了桑色素与黄酮类化合物的结构-亲和力关系。位点标记竞争置换实验表明，桑色素结合位点II（亚结构域IIIA）的BSA具有高亲和力。圆二色谱结果表明桑色素的存在改变了BSA的构象。此外，还考察了几种常见金属离子对桑色素与BSA结合常数的影响。(c)2012 Elsevier B. V.保留所有权利。
The interaction between morin and bovine serum albumin (BSA) was studied using molecular spectroscopic approach at different temperatures under imitated physiological conditions. Quenching of intrinsic tryptophanyl fluorescence of BSA with increasing morin concentration is the actuating tool in the analysis. The obtained quenching mechanisms, binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that the hydrophobic interaction play a major role in the morin-BSA association. Binding affinity between morin and BSA was determined using Scatchard equation and the modified Stern-Volmer equation, and the corresponding Structure-affinity relationships of flavonoids were discussed. Site marker competitive displacement experiments demonstrated that morin binds with high affinity to site II (subdomain IIIA) of BSA. Furthermore, the circular dichroism spectral results indicated that the conformation of BSA changed in the presence of morin. In addition, the effect of some common metal ions on the binding constant between morin and BSA was examined. (c) 2012 Elsevier B.V. All rights reserved.