应用荧光法研究了在不同酸度条件下,巴洛沙星(balofloXacin,BLFX)与牛血清白蛋白(BSA)的荧光猝灭现象,利用荧光猝灭双倒数图计算了巴洛沙星与牛血清白蛋白之间的结合常数,根据Fοrster非辐射能量转移机制计算出巴洛沙星在牛血清白蛋白上的结合距离,并根据热力学参数确定了巴洛沙星与牛血清白蛋白之间的作用力类型,同时采用同步荧光技术考察了巴洛沙星对BSA构象的影响。
In the present paper, a fluorescence method was used to study at different pH the fluorescence quenching of bovine serum albumin (BSA) by its interaction with balofloxacin (BLFX). The interaction association constants of BSA and BLFX were determined from a double reciprocal line Weaver-Burk plot. According to the F6rster dipole-dipole energy transfer, the distance to be measured between the BLFX and tryptophane is 5.09 nm. From thermodynamical coordination it can be judged that the binding power between BLFX and BSA is electrostatic effect. The effect of BLFX on the conformation of BSA was also analyzed by using synchronous fluorescence spectroscopy.