中文摘要：

在模拟生理条件下,应用荧光光谱和表面增强拉曼光谱法对对-香豆酸（p-CA）与人血清白蛋白（HSA）的结合机理进行研究。结果表明,p-CA对HSA的荧光猝灭机制为静态猝灭,并伴有非辐射能量转移。荧光光谱显示,在298,304,310 K下,p-CA与HSA的结合常数（KA）分别为3.41×10~4,2.09×10~4,1.38×10~4L/mol,结合位点数（n）近似为1。表面增强拉曼光谱研究揭示,p-CA的酚基与HSA有效结合。标记竞争实验指出,p-CA在HSA上的结合位点主要在SiteⅠ。反应过程热力学参数表明,二者间的作用主要为静电引力,且根据Frster能量转移理论求得p-CA与HSA间的距离为5.11 nm。同步荧光光谱显示,p-CA的结合没有导致HSA构象发生明显变化。

英文摘要：

Under simulated physiological conditions,the binding mechanism between p-Coumaric acid（ p-CA） and human serum albumin（ HSA） was investigated by fluorescence spectrum and surface enhanced Raman scattering（ SERS）. The results show that the effect between p-CA and HSA is a static fluorescence quenching with Frster＇s non-radioactive energy transformation. At 298,304,310 K,the binding constants（ KA） between p-CA and HSA are 3. 41 × 10~4,2. 09 × 104,1. 38 ×10~4L/mol,the binding site（ n） value is approximate to 1. SERS reveals that the phenolic group of p-CA combines with HSA. Thermodynamic data indicate that the interaction between p-CA and HSA is mainly electrostatic attraction. Marker competition experiments point out that the primary binding site for p-CA is located at site Ⅰ in HSA. According to Frster energy transfer theory,the binding distance between p-CA and HSA is 5. 11 nm. Synchronous fluorescence spectra show that the conformation of HSA does not changed apparently with the addition of p-CA.