姜黄素-嘧啶酮衍生物与BSA相互作用的研究
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摘要
在模拟生理酸度(pH=7.4)的条件下,利用荧光猝灭法研究姜黄素嘧啶酮衍生物6-(4-羟基-3-甲氧基苯)-4-((1Z,3E)-羟基-4-(4-羟基-3-甲氧基苯)-1,3-丁二烯-1-基)嘧啶-2(1H)-硫酮与牛血清白蛋白(BSA)的相互作用.实验结果表明:该药物分子对BSA有强的荧光猝灭作用,其猝灭机理是静态猝灭为主;该药物分子与BSA结合位点数约为1,且其结合能力优于姜黄素;运用热力学方程得出热力学参数(ΔH,ΔS)均小于0,可知药物分子与BSA的相互作用力主要是氢键和范德华作用力.
The interaction of curcumin-pyrimidinone derivatives with bovine serum albumin was investigated by fluorescence quenching method under simulated physiological conditions(pH = 7.4). The experiments indicated that the fluorescence of BSA was quenched by the drug molecule and the quenching mechanism was a static quenching process. The binding sites number of drug molecule and BSA was about 1, and its binding ability was better than curcumin. The thermodynamic para-meters(ΔH, ΔS) of drug molecule and BSA system were obtained by thermo-dynamical formulas under different temperatures. According to experimental data, The thermodynamic parameters were ΔH<0 and ΔS<0, indicating that the binding power of the drug molecule and BSA system were mainly hydrogen bond and Vander Waals force.
The interaction of curcumin-pyrimidinone derivatives with bovine serum albumin was investigated by fluorescence quenching method under simulated physiological conditions(pH = 7.4). The experiments indicated that the fluorescence of BSA was quenched by the drug molecule and the quenching mechanism was a static quenching process. The binding sites number of drug molecule and BSA was about 1, and its binding ability was better than curcumin. The thermodynamic para-meters(ΔH, ΔS) of drug molecule and BSA system were obtained by thermo-dynamical formulas under different temperatures. According to experimental data, The thermodynamic parameters were ΔH<0 and ΔS<0, indicating that the binding power of the drug molecule and BSA system were mainly hydrogen bond and Vander Waals force.
引文
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[4] Wolf,F.A.,Brett,G.M.Ligand-binding proteins:Their potential for application in systems for controlled delivery and uptake of ligands[J].Pharmacol.Rev.,2000,52,207-236.
[5] Xiao,J.,Suzuki,M.,Jiang,X.,et al.Influence of B-ring hydroxylation on interactions of flavonols with bovine serum albumin[J].J.Agric.Food Chem.,2008,56,2350-2356.
[6] Callis,P.R..1La and 1Lb transitions of tryptophan:applications of theory and experimental observations to fluorescence of proteins[J].Methods Enzymol.,1997,278,113-150.
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[12] 邢其毅.基础有机化学[M].北京:高等教育出版社,2005.
[13] Ross,P.D.,Subramanian,S..Thermodynamics of protein association reactions:forces contributing to stability[J].Biochemistry,1981,20:3096-3102.
[14] Shang L.,Jiang X.,Dong S..In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy[J].J.Photochem.Photobiol.A-Chem.,2006,184,93-97.