Isothermal titration calorimetry study of epicatechin binding to serum albumin
Isothermal titration calorimetry study of epicatechin binding to serum albumin
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DOI：
10.1016/j.jpba.2006.02.004
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发表时间：
2006-08-28
影响因子：
3.4
通讯作者：
Green, Rebecca J.
中科院分区：
文献类型：
--
作者：
Frazier, Richard A.;Papadopoulou, Athina;Green, Rebecca J.
采用等温滴定量热法研究了表儿茶素与牛血清白蛋白（BSA）的相互作用。采用假定独立结合位点的结合模型，测定了三种BSA溶液浓度下相互作用的结合常数（K）和相关热力学结合参数（n，Δ H）。这些数据显示表儿茶素与BSA的弱非共价结合。在量热池中，相互作用能随BSA浓度变化，表明表儿茶素的结合诱导BSA聚集。自由能（Δ G）在2 kJ mol（-1）的范围内保持恒定，并且观察到负熵，表明焓驱动的放热相互作用。结果表明，表儿茶素与牛血清白蛋白形成了氢键非共价复合物。(c)2006 Elsevier B. V.保留所有权利。
The interaction of epicatechin with bovine serum albumin (BSA) was studied by isothermal titration calorimetry. The binding constant (K) and associated thermodynamic binding parameters (n, Delta H) were determined for the interaction at three solution concentrations of BSA using a binding model assuming independent binding sites. These data show weak non-covalent binding of epicatechin to BSA. The interaction energetics varied with BSA concentration in the calorimeter cell, suggesting that the binding of epicatechin induced BSA aggregation. The free energy (Delta G) remained constant within a range of 2 kJ mol(-1) and negative entropy was observed, indicating an enthalpy driven exothermic interaction. It is concluded that the non-covalent epicatechin-BSA complex is formed by hydrogen bonding. (c) 2006 Elsevier B.V. All rights reserved.