荧光法研究喹诺酮类抗菌药物和蛋白质的相互作用  被引量:15

Study on the interaction between quinolone and bovine serum albumins by fluorescence

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作  者:刘永明[1] 李桂芝[1] 

机构地区:[1]烟台大学化学院,山东烟台264005

出  处:《化学研究与应用》2005年第1期46-48,共3页Chemical Research and Application

摘  要:用荧光光谱法、分光光度法研究水溶液中甲磺酸培氟沙星、盐酸芦氟沙星与牛血清白蛋白(BSA)的相互结合反应,表明二者以摩尔比1∶1牢固结合,结合的平衡常数分别为KPM=7 3×104L mol、KRH=9 3×104L mol。根据F rster非辐射能量转移机理,求算了甲磺酸培氟沙星、盐酸芦氟沙星与牛血清白蛋白给体-受体间距离r分别为2 82nm,2 93nm,能量转移效率E分别为0 31,0 44。喹诺酮类药物与牛血清白蛋白的相互结合作用为单一的静态猝灭过程,其作用机制为能量转移机制。The binding reaction between bovine serum albumins(BSA) and pefioxacin mesylate(PM) or rufioxacin hydrochloride(RH) in aqueous was studied by fluorescence and UV-Vis absorption spectra.The results indicated that PM and RH strongly bind to BSA with the molar ratio of 1∶1 and the equilibrium constants of K_(PM)=7.2×10~4 L/mol and K_(RH)=9.3×10~4 L/mol respectively.The action distances (r_(PM)=2.82nm,r_(RH)=2.93nm) and energy transfer efficiencies (E_(PM)=0.31,E_(RH)=0.44,)between donor (BSA) and acceptor (PM,RH) were obtained by Frster's nonradiative energy transfer mechanism.The Stern-Volmer curve on the fluorescence of BSA quenched by series of quinolone concentration was linear,which illustrated the combination reaction of quinolone and BSA is a single static quenching process.

关 键 词:甲磺酸培氟沙星 盐酸芦氟沙星 牛血清白蛋白 荧光猝灭 

分 类 号:O557.39[理学—热学与物质分子运动论]

 

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