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 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 Frster’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.展开更多
了解生物活性小分子与血清蛋白之间的相互作用有重要意义。采用激发波长280 nm,检测不同浓度异戊烯根皮苷对BSA在30°C和40°C下300～400 nm范围荧光发射光谱的影响。结果表明,BSA的内源荧光强度随溶液中加入异戊烯根皮苷浓度...了解生物活性小分子与血清蛋白之间的相互作用有重要意义。采用激发波长280 nm,检测不同浓度异戊烯根皮苷对BSA在30°C和40°C下300～400 nm范围荧光发射光谱的影响。结果表明,BSA的内源荧光强度随溶液中加入异戊烯根皮苷浓度的增加呈现有规律的降低,异戊烯根皮苷对BSA荧光猝灭常数Ksv30°C=6.2×103L/m o l,Ksv40°C=5.9×103L/m o l;结合常数K30°C=0.05 m o l/L,K40°C=0.03 m o l/L,结合位点数n30°C=0.64,n40°C=0.76;热力学参数ΔH=42 449.61 kJ.m o l,ΔG=7 543.04 kJ.m o l,ΔS=115.20 J/(m o l.K)。异戊烯根皮苷与BSA产生相互作用,其相互作用机制是异戊烯根皮苷与BSA的结合,并以静电作用力为主。展开更多
文摘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 Frster’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.
文摘了解生物活性小分子与血清蛋白之间的相互作用有重要意义。采用激发波长280 nm,检测不同浓度异戊烯根皮苷对BSA在30°C和40°C下300～400 nm范围荧光发射光谱的影响。结果表明,BSA的内源荧光强度随溶液中加入异戊烯根皮苷浓度的增加呈现有规律的降低,异戊烯根皮苷对BSA荧光猝灭常数Ksv30°C=6.2×103L/m o l,Ksv40°C=5.9×103L/m o l;结合常数K30°C=0.05 m o l/L,K40°C=0.03 m o l/L,结合位点数n30°C=0.64,n40°C=0.76;热力学参数ΔH=42 449.61 kJ.m o l,ΔG=7 543.04 kJ.m o l,ΔS=115.20 J/(m o l.K)。异戊烯根皮苷与BSA产生相互作用,其相互作用机制是异戊烯根皮苷与BSA的结合,并以静电作用力为主。
