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作 者:刘保生[1] 薛春丽[1] 王晶[1] 杨超[1] 吕运开[1]
机构地区:[1]河北大学理化分析中心药物化学与分子诊断教育部重点实验室,河北保定071002
出 处:《发光学报》2010年第2期285-290,共6页Chinese Journal of Luminescence
基 金:国家自然科学基金(200675024)资助项目
摘 要:在pH=7.40的水溶液中,环丙沙星(CPFX)、氧氟沙星(OFLX)能够猝灭牛血清白蛋白(BSA)的荧光。当两种药物共存时BSA荧光被进一步猝灭。据此建立了利用荧光发光光谱法进行喹诺酮类药物CPFX与OFLX间相互作用的研究。结果表明:药物间存在相互作用,使药物与蛋白间的结合常数减小、结合稳定性下降,游离型药物含量增加,造成药效增强;药物对蛋白荧光的猝灭属于静态猝灭,药物与蛋白结合位点数约为1。根据Frster非辐射能量转移理论,确定了药物与蛋白之间的结合距离r<7nm,属于非辐射能量转移。药物间的相互作用使r值增加,结合距离增大。同步荧光光谱研究表明药物间的相互作用对蛋白构象产生影响,使蛋白质分子伸展,疏水性降低。In the aqueous solution of pH=7.40,both ciprofloxacin (CPFX) and ofloxacin (OFLX) can quench fluorescence of bovine serum albumin (BSA).The fluorescence intensity is obviously gone down when the two drugs coexist.According to this,studies were established on the interaction between CPFX and OFLX by fluorescence spectrum.It was proved that the interaction between the drugs reduces the binding stability of the drug and protein.At the same time,increase of the free drug concentration will increase the effect of the drugs.The result showed that the quenching mechanism of the combination of bovine serum albumin and drugs is a static procedure.The number of binding sites is 1 in several of system.Based on the theory of Frester spectroscopy energy transfer,the binding distance (r〈7.0 nm) between the drugs and BSA was obtained.It belongs to non-radiation energy transfer.Because of the existence of interaction between the drugs,the correlation coefficient and binding distance are increased.Studies by synchronous spectra show the effect of the interaction between the drugs on conformation of BSA.It makes protein molecules extend and hydrophobic nature reduces.
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