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在模拟人体生理条件下,用荧光光谱法和紫外-可见吸收光谱法研究氯诺昔康(LNXC)和牛血清白蛋白(BSA)结合反应的特征。研究表明:氯诺昔康与牛血清白蛋白形成复合物,从而猝灭牛血清白蛋白的内源性荧光,该过程为静态猝灭过程。根据Stern-Volmer方程求出不同温度下结合位点数和结合常数;根据Forster非辐射能量转移理论可求出不同温度下的作用距离;通过计算相应的热力学参数,确定了氯诺昔康与牛血清白蛋白之间的作用力主要为静电引力;并利用同步荧光光谱及三维荧光光谱法探讨了氯诺昔康与牛血清白蛋白作用前后白蛋白的构象变化;此外探讨了共存金属离子对氯诺昔康与牛血清白蛋白结合作用的影响。
Fluorescence spectroscopy and UV-Vis absorption spectroscopy were used to study the binding characteristics of lornoxicam (LNXC) and bovine serum albumin (BSA) under simulated human physiological conditions. Studies have shown that lornoxicam forms a complex with bovine serum albumin, thereby quenching the endogenous fluorescence of bovine serum albumin, which is a static quenching process. According to the Stern-Volmer equation, the number of binding sites and the binding constants at different temperatures were calculated. According to the theory of Forster non-radiative energy transfer, the action distances at different temperatures were obtained. By calculating the corresponding thermodynamic parameters, lornoxicam and bovine serum The interaction between albumin and albumin was mainly electrostatic attraction. The conformational changes of albumin before and after lornoxicam and bovine serum albumin were investigated by synchronous fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. In addition, Effect of oxicum and bovine serum albumin binding.