Wu Jin-Xiu, Li Mei, Song Yu-Min, Liu Zhao-Gang, Hu Yan-Hong
College of Rare Earth, Inner Mongolia University of Science and Technology, Baotou 014010, China.
Guang Pu Xue Yu Guang Pu Fen Xi. 2009 Aug;29(8):2199-203.
The binding reaction of rutin-Sm with serum albumin (SA) was investigated by the fluorescence method in physiological condition. The authors studied mainly the quenching mechanism of the fluorescence of SA by rutin-Sm, and calculation of the binding constants K(LB) of human serum albumin (HSA) and bovine serum albumin (BSA) with rutin-Sm by Lineweaver-Burk equation at different temperatures respectively, then obtained the thermodynamic parameters of HSA and BSA with rutin-Sm according to the calculated binding constants K(LB) at different temperature, meanwhile the type of binding forces of HSA and BSA with rutin-Sm was determined. The results showed that the emission spectra of BSA (HSA) in the presence and absence of rutin-Sm are different. The emission spectra of BSA (HSA) in the presence of rutin-Sm can be quenched. The quenching mechanism of rutin-Sm to SA was static quenching with non-radiation energy transfer for new complex of SA and rutin-Sm. The binding constants K(LB) (L x moL(-1)) were 6.540 x 10(5) and 3.265 x 10(5) for BSA, and 6.830 x 10(5) and 4.665 x 10(5) for HSA at 295 K and 310 K respectively. And the type of bonding forces was estimated by the calculation of thermodynamic parameters of the reaction of rutin-Sm with SA at different temperatures, and the result showed that the binding forces were mainly H-bond and Van der Waals between BSA and rutin-Sm due to the deltaH < 0 and deltaS < 0, and the main electrostatic interaction of rutin-Sm and HSA because of deltaH < 0 and deltaS > 0. The effect of rutin-Sm on the conformation of serum albumin was also studied by using synchronous fluorescence spectroscopy. Results indicated that rutin-Sm could be deposited and transported by serum protein in vivo.
在生理条件下，采用荧光法研究了芦丁 - 钐与血清白蛋白（SA）的结合反应。作者主要研究了芦丁 - 钐对SA荧光的猝灭机制，并分别通过Lineweaver - Burk方程计算了人血清白蛋白（HSA）和牛血清白蛋白（BSA）在不同温度下与芦丁 - 钐的结合常数K(LB)，然后根据不同温度下计算得到的结合常数K(LB)获得了HSA和BSA与芦丁 - 钐的热力学参数，同时确定了HSA和BSA与芦丁 - 钐的结合力类型。结果表明，存在和不存在芦丁 - 钐时BSA（HSA）的发射光谱不同。芦丁 - 钐存在时BSA（HSA）的发射光谱会发生猝灭。芦丁 - 钐对SA的猝灭机制是静态猝灭，伴随着SA与芦丁 - 钐新复合物的非辐射能量转移。在295 K和310 K时，BSA的结合常数K(LB)（L×moL(-1)）分别为6.540×10(5)和3.265×10(5)，HSA的结合常数K(LB)分别为6.830×10(5)和4.665×10(5)。通过计算不同温度下芦丁 - 钐与SA反应的热力学参数来估计结合力类型，结果表明，由于ΔH < 0且ΔS < 0，BSA与芦丁 - 钐之间的结合力主要是氢键和范德华力，而由于ΔH < 0且ΔS > 0，芦丁 - 钐与HSA之间主要是静电相互作用。还利用同步荧光光谱研究了芦丁 - 钐对血清白蛋白构象的影响。结果表明，芦丁 - 钐在体内可由血清蛋白储存和转运。
