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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。
Fluorescence spectra and ultraviolet spectra were used to study the spectral behavior of heteropoly acid salt K7 [PTi2W10O40] · 6H2O (PM-19) bound to human serum albumin (HSA) under physiological conditions. It was found that PM-19 had a strong fluorescence quenching effect on HSA. Stern-Volmer and Lineweaver-Burk equations were used to process the experimental data respectively. It was found that HSA reacts with PM-19 to form a new complex which belongs to the static fluorescence quenching. The formation constants KA (298 K: 2.26 × 105 L / mol; 303 K: 1.67 × 105 L / mol; 310 K: 1.01 × 105 L / mol) at different reaction temperatures were calculated from the Lineweaver- The main thermodynamic parameters (ΔH = -51.12kJ / mol; ΔS = -88.19 / -87.85 / -88.26 J / K; ΔG = -24.84 / -24.50 / -23.78kJ / mol) Hydrogen bond and van der Waals forces. According to F rster non-radiative energy transfer mechanism to calculate the distance between the two (4.21 nm). The effect of PM-19 on the conformation of HSA was also investigated by synchronous fluorescence spectroscopy.