CAJ | 학술논문

应用荧光和紫外-可见光谱研究了4个不同pH的Britton-Robinson（B-R）缓冲溶液中洛美沙星与牛血清白蛋白（BSA）的相互作用.应用Stern-Volmer方程、Lineweaver-Burk双倒数方程以及F rster能量转移理论,计算得到4个不同pH下两者结合的猝灭常数（KS）V、结合常数（K）a和结合距离（r）等参数.其结果显示：4个pH下,BSA与洛美沙星均能发生反应生成新的复合物,属于静态荧光猝灭;洛美沙星与BSA间结合距离均小于7 nm;pH对两者的相互结合具有一定的影响,在pH4.9时洛美沙星与BSA结合常数最大,结合距离小;同步荧光光谱显示不同介质中洛美沙星对BSA的构象有比较显著的影响.
응용형광화자외-가견광보연구료4개불동pH적Britton-Robinson（B-R）완충용액중락미사성여우혈청백단백（BSA）적상호작용.응용Stern-Volmer방정、Lineweaver-Burk쌍도수방정이급F rster능량전이이론,계산득도4개불동pH하량자결합적졸멸상수（KS）V、결합상수（K）a화결합거리（r）등삼수.기결과현시：4개pH하,BSA여락미사성균능발생반응생성신적복합물,속우정태형광졸멸;락미사성여BSA간결합거리균소우7 nm;pH대량자적상호결합구유일정적영향,재pH4.9시락미사성여BSA결합상수최대,결합거리소;동보형광광보현시불동개질중락미사성대BSA적구상유비교현저적영향.
The interaction of lomefloxacin and bovine serum albumin（BSA） were studied in the Britton-Robinson buffer with four different pHs by fluorescence spectroscopy and UV-vis spectroscopy.After analyzing the fluorescence quenching data according to Stern-Volmer equation,Lineweaver-Burk double-reciprocal equation and F？rster＇s non-radiation energy transfer mechanism,the quenching constants,binding constants and binding distances were determined at four different pHs.The results showed that BSA had reacted with lomefloxacin and formed a certain new compound.The distances between BSA and lomefloxacin were less than 7 nm.The pH can affect the binding between lomefloxacin and BSA and lomefloxacin has the optimal condition of binding constant and binding distance at pH 4.9.Synchronous fluorescence spectrometry indicated that lomefloxacin remarkable influences on the conformation of BSA in different pH medium.