中文摘要：

用多种光谱技术研究了生理条件下川陈皮素（NOB）与牛血清白蛋白（BSA）的相互作用及热力学特征。结果表明,NOB与BSA有较强的作用,NOB能使BSA的内源荧光猝灭,并以静态猝灭为主。按照Stern-Volmer方程和双对数方程分别得出不同温度下,以及不同pH值时NOB与BSA的结合常数和结合位点数。运用紫外光谱获得常温下NOB与BSA的结合常数与荧光光谱测定值相近,热力学参数△H、△S分别为55.91 kJ.mol^-1、274.61 J.mol^-1.K^-1,表明其主要作用力为疏水力,NOB与BSA作用为非辐射能量转移机制,其能量转移效率与结合距离分别为0.27和1.76 nm,用参比法得出BSA荧光量子产率为0.074。同步荧光光谱研究发现川陈皮素对牛血清白蛋白构象几乎没有影响。

英文摘要：

The interaction between bovine serum albumin（BSA） and nobiletin（NOB） and its thermodynamic characteristics were investigated by multi-spectroscopy in physiological medium.The results showed that NOB could quench the fluorescence of BSA with a static quenching mechanism.The apparent binding constants and the number of binding sites at different temperatures and different pH values were estimated according to Stern-Volmer equation and double logarithmic equation,respectively.The binding constant of NOB to BSA was also estimated at room temperature using UV-Vis method, which is similar to that obtained by fluorescence analysis. The thermodynamic parameters AH and AS were estimated as 55.91 kJ·mo1^-1 and 274.61 J·mol^-1· K^-1, indicating that the hydrophobic force of NOB and BSA is mainly interaction force. The fluorescence quantum yield of BSA was calculated as 0. 074. According to Fǒrster theory, the energy transfer efficiency and the binding distance of NOB to BSA were 0.27 and 1.76 nm, respectively. Synchronous fluorescence spectra of BSA indicated that NOB didn＇t affect the conformation of BSA.