A calorimetric study on interactions of colchicine with human serum albumin

被引:24
作者
Zhao, Qiang [1 ]
Xu, Xiang-Yu [1 ]
Sun, Xiang-Jun [1 ]
Liu, Min [1 ]
Sun, De-Zhi [1 ]
Li, Lin-Wei [1 ]
机构
[1] Liaocheng Univ, Coll Chem & Chem Engn, Liaocheng 252059, Shandong, Peoples R China
基金
中国国家自然科学基金;
关键词
Isothermal titration calorimetry; Colchicine; Human serum albumin; AQUEOUS-SOLUTIONS; BINDING-SITES; CYCLODEXTRIN; SURFACTANTS;
D O I
10.1016/j.molstruc.2009.05.026
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Interaction of colchicine (COL) with human serum albumin (HSA) in buffer solutions (pH 7.2) has been investigated by isothermal titration calorimetry (ITC) combined with circular dichroism (CD) and UV-vis spectra. Heats of the interactions have been determined at 298.15 K. Based on the calorimetric data and reasonable suppositions for the bio-macromolecule - ligand binding process, the equilibrium constants, standard changes of enthalpy, entropy and Gibbs free energy of the processes are obtained. The results show that there are two classes of ligand binding sites. The first-class binding is mainly driven by entropy, while the second-class binding is synergistically driven by entropy and enthalpy. Circular dichroism (CD) and UV-vis spectra show that COL can change the secondary structure of HSA molecule. (C) 2009 Elsevier B.V. All rights reserved.
引用
收藏
页码:31 / 34
页数:4
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