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采用荧光光谱法研究了在模拟人体生理环境条件下,pH 7.40的Tris-HCl缓冲体系中,丹酚酸A(Sal A)与牛血清白蛋白(BSA)的相互作用。结果表明,丹酚酸A对牛血清白蛋白有较强的荧光猝灭作用。用Stern-Volmer和Lineweaver-Burk方程处理数据,推断其猝灭机理为丹酚酸A与牛血清白蛋白形成复合物的静态猝灭,并获得了25、30、35℃下丹酚酸A与牛血清白蛋白作用的结合常数分别为1.49×105、1.19×105、8.24×104 L/mol。根据Van’t Hoff方程计算得出ΔH=-56.55kJ/mol,根据所得热力学参数推断丹酚酸A与牛血清白蛋白之间的主要作用力为氢键与范德华力。在25℃时,计算获得丹酚酸A与牛血清白蛋白的结合位点数为1.158。
Fluorescence spectroscopy was used to study the interaction between SalA and bovine serum albumin (BSA) in Tris-HCl buffer pH 7.40 under simulated physiological conditions. The results showed that salvianolic acid A had a strong fluorescence quenching effect on bovine serum albumin. Data were processed by Stern-Volmer and Lineweaver-Burk equations, and the quenching mechanism was deduced to be the static quenching of the complex formed between salvianolic acid A and bovine serum albumin. The results showed that salvianolic acid A at 25,30 and 35 ℃ The binding constants of bovine serum albumin were 1.49 × 105, 1.19 × 105 and 8.24 × 104 L / mol, respectively. Based on the Van’t Hoff equation, ΔH = -56.55 kJ / mol was calculated, and the main interactions between salvianolic acid A and bovine serum albumin were concluded as hydrogen bond and van der Waals forces based on the obtained thermodynamic parameters. At 25 ° C, the number of binding sites for salvianolic acid A and bovine serum albumin was calculated to be 1.158.