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同步荧光法研究胺菊酯与牛血清白蛋白的相互作用 被引量:4

Study of the interaction between tetramethrin and bovine serum album by synchronous fluorescence spectroscopy
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摘要 The synchronous fluorescence spectrometry was used for the first time to eliminate the interference between the emission of the small-molecule drugs and the determination of the endogenous fluorescence of the protein.The synchronous fluorescence spectrometry and UV-Vis were applied to study the interaction between Tetramethrin and BSA in physiological buffer(pH 7.4).The results of the experiment proved that the quenching mechanism of fluorescence of BSA by Tetramethrin was a static quenching procedure.The number of binding potential point(n) and the association constant(K0) at 298K were n=1.13 and K0=1.428×105L·mol-1,respectively.The enthalpy change and the entropy change were calculated to be △H=29.69KJ·mol-1,△S=211.65J·K·mol-1,which showed that the binding mode was mainly the reflection of the hydrophobic interaction.On the basis of the Frster’s non-radiative energy transfer mechanism,the binding distance(r) and the rate of energy transfer(E)between donor(BSA) and acceptor(Tetramethrin) were obtained to be r=5.15nm,E=0.117,respectively. The synchronous fluorescence spectrometry was used for the first time to eliminate the interference between the emission of the small-molecule drugs and the determination of the endogenous fluorescence of the protein.The synchronous fluorescence spectrometry and UV-Vis were applied to study the interaction between Tetramethrin and BSA in physiological buffer(pH 7.4).The results of the experiment proved that the quenching mechanism of fluorescence of BSA by Tetramethrin was a static quenching procedure.The number of binding potential point(n) and the association constant(K0) at 298K were n=1.13 and K0=1.428×105L·mol-1,respectively.The enthalpy change and the entropy change were calculated to be △H=29.69KJ·mol-1,△S=211.65J·K·mol-1,which showed that the binding mode was mainly the reflection of the hydrophobic interaction.On the basis of the Frster's non-radiative energy transfer mechanism,the binding distance(r) and the rate of energy transfer(E)between donor(BSA) and acceptor(Tetramethrin) were obtained to be r=5.15nm,E=0.117,respectively.
出处 《化学研究与应用》 CAS CSCD 北大核心 2010年第6期763-766,共4页 Chemical Research and Application
基金 山东省科技攻关项目(2009GG10009053)资助
关键词 胺菊酯 牛血清白蛋白 同步荧光法 荧光猝灭 紫外可见光谱法 tetramethrin bovine serum album synchronous fluorescence spectometry fluorescence quenching UV-Vis spectra
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