合成了白杨素磺酸钠和白杨素磺酸钙两种白杨素磺酸盐衍生物,并分别采用荧光光谱法研究了它们与牛血清白蛋白(BSA)的相互作用。结果表明：两种白杨素磺酸盐对BSA有较强的荧光猝灭作用,根据Stern-Volmer方程得到的荧光猝灭常数,可判断由于与白杨素磺酸盐反应而导致BSA的荧光猝灭均属于静态猝灭。采用位点结合模型公式和Frster非辐射能量转移理论计算了结合常数、结合位点数、结合距离。从计算得到的热力学参数焓变ΔH和熵变ΔS,推断了白杨素磺酸钠与BSA之间的作用力为静电引力,而白杨素磺酸钙与BSA之间的作用力为氢键和范德华力。并应用同步荧光技术研究了白杨素磺酸盐对BSA构象的影响。

Two chrysin-8-sulfonates (i.e., sodium chrysin-8-sulfonate and calcium chrysin-8-sulfonate) were synthesized, and mechanism of the interaction between two chrysin-8-sulfonates and bovine serum albumin (BSA) was studied by fluorospectrometry. Significant quenching of fluorescence of BSA was found by its reaction with two chrysin-8-sulfonates. As judged from the fluorescence quenching constants obtained by Stern-Volmer equation, fluorescence quenching of BSA by chrysin-8-sulfonates was attributed to static quenching. The binding constants, number of binding sites and binding distance were found by applying the equation of site-binding model and Frster′s nonradiative energy transfer theory. Values of thermodynamic parameters ΔH and ΔS were calculated and based on these results, the binding force between sodium chrysin-8-sulfonate and BSA was recognized to be electrostatic attraction, and the binding force between calcium chrysin-8-sulfonate and BSA was hydrogen bond and Vander Waals force.