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在模拟生理条件下,用荧光光谱法和紫外-可见吸收光谱法研究头孢硫脒和牛血清白蛋白(BSA)结合反应的特征。研究表明:头孢硫脒与牛血清白蛋白形成复合物,从而猝灭BSA的内源性荧光,该过程为静态猝灭过程。根据Stern-Volmer方程得出了不同温度下结合位点数n和结合常数Ka;结合位点位于BSA的亚结构ⅡA中。通过计算相应的热力学参数,确定了头孢硫脒与牛血清白蛋白之间的作用力主要为氢键和范德华力。利用同步荧光光谱探讨了头孢硫脒与BSA作用前后BSA的构型变化。Hill系数nH<1,表明头孢硫脒有弱的负协同作用。此研究不仅对于揭示体内药物动力学问题和指导临床合理用药具有一定意义,而且对药物分子设计及新药开发等也具有重要指导意义。
Under simulated physiological conditions, the binding characteristics of cefathiamidine and bovine serum albumin (BSA) were studied by fluorescence spectroscopy and UV-Vis absorption spectroscopy. Studies have shown that cefathiamidine forms a complex with bovine serum albumin, thereby quenching the endogenous fluorescence of BSA, which is a static quenching process. Based on the Stern-Volmer equation, the number of binding sites n and the binding constant Ka at different temperatures were obtained. The binding sites were located in sub-structure IIA of BSA. By calculating the corresponding thermodynamic parameters, it was confirmed that the interaction between cefathiamidine and bovine serum albumin was hydrogen bond and van der Waals forces. The conformational changes of BSA before and after cefathiamidine and BSA were investigated by synchronous fluorescence spectroscopy. Hill coefficient nH <1, indicating that cefathiamidine has a weak negative synergistic effect. This study is not only meaningful for revealing the in vivo pharmacokinetic problems and guiding clinical rational use of drugs, but also has important guiding significance for the design of drug molecules and the development of new drugs.