A Thermodynamic Study on the Binding of PEG-Stearic Acid Copolymer with Lysozyme
A Thermodynamic Study on the Binding of PEG-Stearic Acid Copolymer with Lysozyme
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DOI：
10.1007/s10953-008-9360-5
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发表时间：
2009-02-01
影响因子：
1.2
通讯作者：
Hekmat, A.
中科院分区：
文献类型：
--
作者：
Behbehani, G. Rezaei;Divsalar, A.;Hekmat, A.
用等温滴定量热法研究了在pH=7.0、温度为27℃的磷酸盐缓冲溶液中，硬脂酸与聚乙二醇400共聚物S400与溶菌酶相互作用的热力学。扩展溶剂化模型被用来再现S400+溶菌酶相互作用的热焓。从扩展溶剂化模型中恢复的溶剂化参数归因于溶菌酶的结构变化和生物活性。S400与溶菌酶相互作用的结合参数表明，在低浓度S400时，溶菌酶结构不稳定，但在较高浓度时，溶菌酶结构被S400稳定。推测S400与溶菌酶上的一组三个相同的结合部位相互作用。
The thermodynamics of the interaction between a copolymer of polyethyleneglycol400-stearic acid, S400, and lysozyme was investigated at pH=7.0 and 27 A degrees C in phosphate buffer by isothermal titration calorimetry, ITC. The extended solvation model was used to reproduce the enthalpies of the S400 + lysozyme interactions. The solvation parameters recovered from the extended solvation model are attributed to the structural change of lysozyme and its biological activity. The binding parameters found for the interaction of S400 with lysozyme indicate that at low concentrations of S400, the lysozyme structure was destabilized but at higher concentrations of S400 lysozyme it was stabilized by S400. It is suggested that S400 interacts with a set of three identical binding sites on lysozyme.