摘要
在模拟动物体生理条件下,用荧光和紫外光谱研究了在不同温度下杂多酸盐K7[PTi2W10O40]·6H2O(PM-19)与人血清白蛋白(HSA)结合反应的光谱行为。试验发现,PM-19对HSA有较强的荧光猝灭作用。用Stern-Volmer和Lineweaver-Burk方程分别处理试验数据,发现HSA与PM-19发生反应生成了新的复合物,属于静态荧光猝灭。由Lineweaver-Burk方程求出了不同温度下反应时复合物的形成常数KA(298 K:2.26×105L/mol;303 K:1.67×105L/mol;310K:1.01×105L/mol)及对应温度下结合反应的热力学参数(ΔH=-51.12kJ/mol;ΔS=-88.19/-87.85/-88.26 J/K;ΔG=-24.84/-24.50/-23.78kJ/mol),证明二者之间的主要作用力氢键和范德华力。根据F rster非辐射能量转移机制计算出了两者之间作用距离(4.21 nm)。同时用同步荧光光谱法探讨了PM-19对HSA构象的影响。
The interaction of salt of heteropoly acid (PM-19) with human serum albumin (HSA) was studied by fluorescence and ultraviolet spectrometry under simulative physiological conditions. The binding of PM-19 to HSA quenched the fluorescence emission from HSA and the results showed that static quenching occurred together with complex formation. The binding constants of the complex at different temperatures KA(298 K: 2.26 ×10^5 L/mol; 303 K: 1.67 ×10^5 L/mol; 310 K: 1.01×10^5L/mol) and the thermodynamic parameters (△H = -51.12 kJ/mol; △S = - 88.19/- 87.85/- 88.26 J/K; △G = - 24.84/- 24.50/- 23.78 kJ/mol) at correspondence temperatures were obtained according to Lineweaver-Burk equation. The latter indicated hydrogen bond and Van der Waar's forces played major roles in the binding of PM-19 to HSA. The binding distance was an are of 4.21 nm based on Forster's non-radiation energy transfer mechanism. The effect of PM-19 on the conformation of HSA was analyzed by synchronous fluorescence spectroscopy.
出处
《分析试验室》
CAS
CSCD
北大核心
2007年第12期98-101,共4页
Chinese Journal of Analysis Laboratory
基金
国家自然科学基金(20271024)项目资助
关键词
杂多酸盐
人血清白蛋白
荧光光谱
紫外光谱
热力学参数
同步荧光光谱
Salt of heteropoly acid
Human serum albumin
Thermodynamic parameter
Fluorescence spectroscopy
Synchronous fluorescence spectroscopy