邻苯二甲酸二乙酯与牛血清白蛋白相互作用的光谱学研究
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摘要
采用荧光光谱法与紫外光谱法研究了邻苯二甲酸二乙酯(DEP)与牛血清白蛋白(BSA)之间的相互作用机制。荧光猝灭结果表明,在模拟生理条件(pH=7.4)下,DEP对BSA主要为静态猝灭过程;298 K时的结合常数与结合位点数分别为2.69×10~4 L·mol~(-1)和0.93;热力学参数焓变(ΔH)与熵变(ΔS)均为正数,说明DEP与BSA之间主要为疏水作用力。依据F?rster非辐射能量转移理论求得DEP与BSA之间的结合距离为2.12nm,两者之间极有可能发生非辐射能量转移,由紫外光谱、同步荧光光谱和三维荧光光谱实验结果可知DEP诱导BSA分子构象发生变化。
The interaction mechanism between diethyl phthalate(DEP)and bovine serum albumin(BSA)was studied using fluorescence and UV spectroscopy.The results of fluorescence quenching showed that,the fluorescence of BSA was quenched by DEP through a static quenching procedure under simulated physiological conditions(pH=7.4).The binding constant and binding site number were 2.69×10~4 L·mol~(-1 )and 0.93 at 298 K,respectively.The thermodynamic parameters enthalpy change(ΔH)and entropy change(ΔS)were both positive,indicating that the interaction of DEP with BSA was driven mainly by hydrophobic forces.According to the F?rster non-radiative energy transfer theory,the binding distance between DEP and BSA is 2.12 nm,which indicated that the energy transfer from BSA to DEP occurs with high possibility.The changes of BSA secondary structure in the presence of DEP were studied by UV spectroscopy,synchronous fluorescence spectrum and three-dimensional fluorescence spectrum.The results indicated that the binding of DEP to BSA induced conformational changes in BSA.
The interaction mechanism between diethyl phthalate(DEP)and bovine serum albumin(BSA)was studied using fluorescence and UV spectroscopy.The results of fluorescence quenching showed that,the fluorescence of BSA was quenched by DEP through a static quenching procedure under simulated physiological conditions(pH=7.4).The binding constant and binding site number were 2.69×10~4 L·mol~(-1 )and 0.93 at 298 K,respectively.The thermodynamic parameters enthalpy change(ΔH)and entropy change(ΔS)were both positive,indicating that the interaction of DEP with BSA was driven mainly by hydrophobic forces.According to the F?rster non-radiative energy transfer theory,the binding distance between DEP and BSA is 2.12 nm,which indicated that the energy transfer from BSA to DEP occurs with high possibility.The changes of BSA secondary structure in the presence of DEP were studied by UV spectroscopy,synchronous fluorescence spectrum and three-dimensional fluorescence spectrum.The results indicated that the binding of DEP to BSA induced conformational changes in BSA.
引文
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[3]张彪,冯统新,关英俊,等.邻苯二甲酸二乙酯检测方法研究进展[J].中国卫生检验,2017,27(22):3336-3340.
[4]周益奇,刘云霞.北京市污水处理厂中邻苯二甲酸酯污染水平及其趋势[J].环境科学,2013,34(4):1357-1362.
[5]龚含情,陈建波.利用光谱法和分子对接技术研究4-乙基-2-甲氧基苯酚与人血清白蛋白之间的相互作用[J].光谱学与光谱分析,2018,38(6):1869-1873.
[6]Shanmugaraj K,Anandakumar S,Ilanchelian M.Probing the binding interaction of thionine with lysozyme:A spectroscopic and molecular docking investigation[J].Dyes Pigments,2014,7(3):210-219.
[7]Teng Y,Wang X,Zou L Y,et al.Experimental and theoretical study on binding of 2-mercaptothiazoline to bovine serum albumin[J].J Lumin,2015,12(46):14-19.
[8]Molina-Bolívar J A,Galisteo-González F,Carnero Ruiz C,et al.Spectroscopic investigation on the interaction of maslinic acid with bvovine serun ablumin[J].J Lumin,2014,8(11):141-149.
[9]Tian Zhiyong,Zang Fenglei,Luo Wen,et al.Spectroscopic study on the interaction between mononaphthalimide spermidine(MINS)and bovine serum albumin(BSA)[J].J Photoch Photobio b,2015,142:103-109.
[10]Cheng Z J,Zhang Y T.Spectroscopic investigation on interaction of salidroside with bovine serum albumin[J].J Mol Struct,2008,1(13):20-27.
[11]孙洋,樊君,胡晓云,等.荧光素钠与牛血清蛋白相互作用的荧光光谱研究及其分析应用[J].化学学报,2011,69(8):937-944.
[12]Gholami S,Bordbar A-K.Exploring binding properties of naringenin with bovine β-lactoglobulin:A fluorescence,molecular docking and molecular dynamics simulation study[J].Biophys Chem,2014,1(3):33-42.
[13]Samanta A,Jana S,Ray D,et al.Modulated photophysics of a cationic DNA-staining dye inside protein bovine serum albumin:Study of binding interaction and structural changes of protein[J].Spectrochimica Acta A:2013,10(49):23-34.
[14]Li X,Jiang J H,Xiao S X,et al.Synthesis,thermodynamic properties and BSA interaction of a new Valen Shiff base derived from o-vanillin and trimethoprim[J].Thermochimica Acta,2013,11(15):291-299.
[15]Cheng Z J,Zhao H M,Xu Q Y,et al.Investigtion of the interaction between indigotin and two serum albumins by spectroscopic approaches[J].J Phacal Ana,2013,3(4):257-269.
[16]Sharma A S,Anandakumar S,Ilanchelian M.A combined spectroscopic and molecular docking study on site selective binding interaction of Toluidine blue O with Human and Bovin serum albumins[J].J Lumin,2014,2(9):206-218.
[17]Li X G,Wang G K,Chen D J,et al.β-Carotene and astaxanthin with human and bovine serum albumins[J].Food Chem,2015,1(133):213-221.
[18]Shi J H,Wang J,Zhu Y Y,et al.Characterization of interaction between isoliquiritigenin and bovine serum albumin:Spectroscopic and molecular docking methods[J].J Lumin,2014,8(42):643-650.
[19]Li Y S,Ge Y S,Zheng Y,et al.Interaction of coomassie brilliant bule G250 with human serum albumin:Probing of the binding mechanism and binding site spectroscopic and molecular modeling methods[J].J Mol Struct,2010,1(15):24-31.
[20]Guo X J,Li X Z,Jiang Y C,et al.A spcetroscopic study on the interaction between p-nitrophenol and bovine serum albumin[J].J Lumin,2014,1(36):353-360.
[21]Li Q,Yang W Y,Qu L L,et al.Interaction of Warfarin with serum albumin and effect of ferulic acid on the binding[J].J Spectrosc,2014,13:1-7.