毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用

吕达, 郭明, 边平凤. 毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用[J]. 环境化学, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
引用本文: 吕达, 郭明, 边平凤. 毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用[J]. 环境化学, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
LYU Da, GUO Ming, BIAN Pingfeng. Studies on the interaction of phthalate esters with bovine serum albumin by capillary electrophoresis[J]. Environmental Chemistry, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
Citation: LYU Da, GUO Ming, BIAN Pingfeng. Studies on the interaction of phthalate esters with bovine serum albumin by capillary electrophoresis[J]. Environmental Chemistry, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704

毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用

  • 基金项目:

    国家自然科学基金(20877072)和浙江省自然科学基金(LY14E030016)资助.

Studies on the interaction of phthalate esters with bovine serum albumin by capillary electrophoresis

  • Fund Project: Supported by the National Natural Science Foundation of China(20877072)and National Natural Science Foundation of Zhejiang Province(LY14E030016).
  • 摘要: 利用毛细管电泳(Capillary electrophoresis,CE)建立邻苯二甲酸二甲酯(Dimethyl Phthalate,DMP)-牛血清白蛋白(Bovine Serum Albumin,BSA)相互作用的分析方法.构建配体DMP-受体BSA相互作用模型.通过区段-区段动力学法(Plug-plug kinetic,PPK),HD法(Hummel-Dreyer,HD),前沿分析法(Frontal analysis,FA)和空峰法(Vacant peak,VP)测定DMP与BSA的相互作用,分别运用Scatchard方程,Klotz方程和非线性方程(Non-linear regression)等理论方法获取两者的相互作用参数,进而分析理论模型适用度.结果表明,PPK法、HD法与FA法都适用于DMP-BSA体系相互作用的测定,HD法最优.模型适用度分析得出非线性回归方程为最适合的理论模型.相互作用参数测试表明DMP-BSA只有单一类型的结合位点且结合强度适中,DMP-BSA分子水平的测定结果可为DMP毒理机制的深入研究提供有益参考.
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  • [1] WILINSON J L, HOODA P S, BARKER J. Ecotoxic pharmaceuticals, personal care products and other emerging contaminants:A review of environmental receptor-mediated, developmental, and epigenetic toxicity with discussion of proposed toxicity to humans[J]. Critical Reviews in Environmental Science and Technology, 2016, 46:336-381.
    [2] VARSHNEY A, SEN P, AHMAD E, et al. Ligand binding strategies of human serum albumin:How can the cargo be utilized?[J]. Chirality, 2010, 22(1):77-87.
    [3] RYAN A J, GHUMAN J, ZUNSZAIN P A, et al. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin[J]. Journal of Structural Biology, 2011, 174(1):84-91.
    [4] WAGNER S, ROTHWEILER F, ANHORN M G, et al. Enhanced drug targeting by attachment of an anti alphav integrin antibody to doxorubicin loaded human serum albumin nanoparticles[J]. Biomaterials, 2010, 31(8):2388-2398.
    [5] SHIBUKAWA A, ISHIZAWA A, KIMURA T, et al. Plasma protein binding study of oxybutynin by high-performance frontal analysis[J]. Journal of Chromatography B, 2002, 768:177-188.
    [6] DUAN L, YANG L J, XIONG H Y, et al. Studies on the electrochemistry of rutin and its interaction with bovine serum albumin using a glassy carbon electrode modified with carbon-coated nickel nanoparticles[J]. Microchimica Acta, 2013, 180(5-6):355-361.
    [7] BOURASSA P, KANAKIS C D, TARANTILIS P, et al. Resveratrol, and curcumin bind serum albumin[J]. The Journal of Physical Chemistry B, 2010, 114(9):3348-3354.
    [8] KUMAR H, BEHAL I. Volumetric, ultrasonic and UV absorption studies on interactions of antibiotric drug chloramphenicol with glycine and its dipeptide in aqueous solutions at T=(288.15-318.15)K[J]. The Journal of Chemical Thermodynamics, 2016, 99:16-29.
    [9] KARTHIKEYAN S, BHARANIDHARAN G, MANI K A, et al. Determination on the binding of thiadiazole derivative to human serum albumin:A spectroscopy and computational approach[J]. Journal of Biomolecular Structure and Dynamics, 2016, 34:1-26.
    [10] GHOSH K, RATHI S, ARORA D, et al. Fluorescence spectral studies on interaction of fluorescent probes with Bovine serum Albumin(BSA)[J]. Journal of Luminescence, 2016, 175:135-140.
    [11] ISLAM M M, SONU V K, GASHNG P M, et al. Caffeine and sulfadiazine interact differently with human serum albumin:A combined fluorescence and molecular docking study[J]. Spectrochimica Acta Part A:Molecular and Biomolecular Spectroscopy, 2016, 152(5):23-33.
    [12] FABINI E, FIORI G M L, TEDESCO D, et al. Surface plasmon resonance and circular dichroism characterization of cucurbitacins binding to serum albumins for early pharmacokinetic profiling[J]. Journal of Pharmaceutical and Biomedical Analysis, 2016, 122(15):166-172.
    [13] VUIGNIER K, SCHAPPLER J, VEUTHEY J L, et al. Drug-protein binding:A critical review of analytical tools[J]. Analytical of Bioanalytical Chemistry, 2010, 398:53-66.
    [14] DEY B, THUKRAL S, KRISHNAN S, et al. DNA-Protein interactions:methods for detection and analysis[J]. Molecular and Cellular Biochemistry, 2012, 365:279-299.
    [15] 郭明, 刘咪咪, 李铭慧, 等. 不同形态铬离子与牛血清白蛋白结合的反应机制[J]. 环境化学, 2013,32(1):65-70.

    GUO M, LIU M M, LI M H, et al. Binding interaction mechanism between different forms of chromiumion and bovine serum albumin[J]. Environmental Chemistry, 2013,32(1):65-70(in Chinese).

    [16] 张礼和, 王梅祥. 化学生物学进展[M]. 北京:化学工业出版社, 2005. ZHANG L H, WANG M X. Advances in Chemicobiology[M]. Beijing:Chemical Indusry Press, 2005(in Chinese).
    [17] ROTSCHAFER J C, ANDES D R, RODVOLD K A. Antibiotic Pharmacodynamics[M]. New York:Humana Press, 2016:109-125.
    [18] LLKHANI H, HUGHES T, Li J, et al. Nanostructured SERS-electrochemical biosensors for testing of anticancer drug interactions with DNA[J]. Biosensors and Bioelectronics, 2016, 80:257-264.
    [19] BOWATER R P, COBB A M, Pivonkova H, et al. Biophysical and electrochemical studies of protein-nucleic acid interactions[J]. Monatshefte für Chemie-Chemical Monthly, 2015, 146:723-739.
    [20] 郭明, 何玲, 孙一新, 等. 槲皮素修饰玻碳电极(Qu/GCE)的制备及铜离子-牛血清白蛋白结合反应机制研究[J]. 环境化学, 2012, 31(9):1355-1361.

    GUO M, HE L, SUN Y X, et al. Investigation of the binding interaction between copper ions and bovine serum albumin on quercetin-modified glassy carbon electrode[J]. Environmental Chemistry, 2012, 31(9):1355-1361(in Chinese).

    [21] ASSFALG M, RAGONA L, PAGANO K, et al. The study of transient protein-noonopartical interactions by solution NMR spectroscopy[J]. Biochimica et Biophysica Acta(BBA)-Protein and Proteomics, 2016, 1864:102-114.
    [22] ZOU J, LEE L T, WANG Q Y, et al. Mapping the interactions between the NS4B and NS3 protein of Dengue Virus[J]. Journal of Virology, 2015, 89:3471-3483.
    [23] 袁东. 分子水平上研究邻苯二甲酸酯及稀土离子类污染物对血清白蛋白的毒性分析新方法[D]. 济南:山东大学, 2011. YUAN D. New methods for the toxicity analysis of pathalate esters and rare earths with serum albumin at the level of molecule[D]. Jinan:Shandong University, 2011(in Chinese).
    [24] 谢晓芸. 几种典型内分泌干扰物与人血清白蛋白相互作用的研究[D]. 兰州:兰州大学, 2011. XIE X Y. The studies of interaction between several typical endocrine disruptors and human serum albumin[D]. Lanzhou:Lanzhou University, 2011(in Chinese).
    [25] 周喜敏. 某些有机小分子与人血清白蛋白的相互作用的研究[D].兰州:兰州大学, 2012. ZHOU X M. Study on interaction between some small organic molecule and human serum albumin[D]. Lanzhou:Lanzhou University, 2012(in Chinese).
    [26] 王亚萍. 农药、塑化剂与蛋白质的结合机理研究[D]. 南昌:南昌大学, 2015. WANG Y P. Investigation on the binding mechanism of pesticides and plasticizer with protein[D]. Nanchang:Nanchang University, 2015(in Chinese).
    [27] DEEB S E, WÄTZIG H, EL-HADY D A, et al. Recent advances in capillary electrophoretic migration techniques for pharmaceutical analysis(2013-2015)[J]. Eletrophoresis, 2016, 37:879.
    [28] KLODZINSKA E, JAWORSKI M, KUPCZYK W. A study of interactions between bacteria and antibiotics by capillary electrophoresis[J]. Electrophoreisis, 2012, 33:3095-3100.
    [29] REDWEIK S, CIANCIULL C, HARA M, et al. Precise fast and flexible determination of protein interactions by affinity capillary electrophoresis. Part 2:Cations[J]. Electrophoresis, 2013, 34:1812-1819.
    [30] ZHANG S, CHENG J, CHEN W J, et al. Interaction between thrombin and natural products of Millettianitita var. hirsutissima using capillary zone electrophoresis[J]. Journal of Chromatrography B, 2009, 877:4107-4114.
    [31] YANG R, ZENG H J, LI J J, et al. Capillary electrophoresis coupled with end-column electrochemiluminescence for the determination of ephedrine in human urine, and a study of its interactions with three proteins[J]. Luminescence, 2011, 26:374-379.
    [32] 燕高峰, 毛伟峰, 贾旭东, 等. 两种邻苯二甲酸酯类物质的抗雄激素作用研究[J]. 中国食品卫生杂志, 2016, 28(2):149-154.

    YAN G F, MAO W F, JIA X D, et al. Study of anti-androgenic effect of two of phthalate esters[J]. Chinese Journal of Food Hygiene, 2016, 28(2):149-154(in Chinese).

    [33] 陈文婕, 戴红, 陈敏, 等. 邻苯二甲酸二乙基己酯(DEHP)对小白鼠肝脏毒性及脂质过氧化损伤[J]. 生态毒理学报, 2012, 7(1):93-98.

    CHEN W J, DAI H, CHEN M, et al. Hepatotoxic effect and lipid oxidative damage of diethylhexyl phthalate(DHEP) on mice[J]. Asian Journal of Ecotoxicology, 2012, 7(1):93-98(in Chinese).

    [34] 武宗高, 陈素燕, 周培源, 等. 3种增塑剂单独和联合暴露对MCF-7细胞增殖的影响[J]. 安全与环境学报, 2015, 15(6):392-395.

    WU Z G, CHEN S Y, ZHOU P Y, et al. Study on the combined effect of the three kinds of plasticizers on the proliferations of MCF-7 cells[J]. Journal of Safely and Environment, 2015, 15(6):392-395(in Chinese).

    [35] DE WITTE W E, WONG Y C, NEDERPELT I, et al. Mechanistic models enable the rational use of in vitro drug-target binding kinetics for better drug effects in patients[J]. Expert Opinion on Drug Discovery, 2016, 11(1):45-63.
    [36] SCATCHARD G, ANN N Y. The attractions of proteins for small molecules and ions[J]. Annals of the New York Academy of Sciences, 1949, 51:660-672.
    [37] KLOTZ I M, HUNSTON D L. Properties of graphical representations of multiple classes of binding sites[J]. Biochemistry, 1971, 10:3065-3069.
    [38] 刘春叶, 张雪娇, 苗延青, 等. 毛细管电泳法研究牛血清白蛋白与盐酸异丙肾上腺素的相互作用[J]. 分析科学学报, 2015, 31(3):313-317.

    LIU C Y, ZHANG X J, MIAO Y Q, et al. Studies on the interaction between bovine serum albumin and hydrochloric acid isoproterenol by capillary electrophoresis[J]. Journal of Analytical Science, 2015, 31(3):313-317(in Chinese).

    [39] XIA Z N, LI L X, CHEN H, et al. Kinetic parameters of interaction between cell membrane and drug by ppkce[J]. Chemical Journal of Chinese Universities, 2011, 32:851-856.
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  • 收稿日期:  2016-06-27
  • 刊出日期:  2017-03-15
吕达, 郭明, 边平凤. 毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用[J]. 环境化学, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
引用本文: 吕达, 郭明, 边平凤. 毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用[J]. 环境化学, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
LYU Da, GUO Ming, BIAN Pingfeng. Studies on the interaction of phthalate esters with bovine serum albumin by capillary electrophoresis[J]. Environmental Chemistry, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704
Citation: LYU Da, GUO Ming, BIAN Pingfeng. Studies on the interaction of phthalate esters with bovine serum albumin by capillary electrophoresis[J]. Environmental Chemistry, 2017, 36(3): 496-507. doi: 10.7524/j.issn.0254-6108.2017.03.2016062704

毛细管电泳法研究邻苯二甲酸酯与牛血清白蛋白分子的相互作用

  • 1.  浙江农林大学化学系, 临安, 311300;
  • 2.  浙江大学化学系, 杭州, 310027
基金项目:

国家自然科学基金(20877072)和浙江省自然科学基金(LY14E030016)资助.

摘要: 利用毛细管电泳(Capillary electrophoresis,CE)建立邻苯二甲酸二甲酯(Dimethyl Phthalate,DMP)-牛血清白蛋白(Bovine Serum Albumin,BSA)相互作用的分析方法.构建配体DMP-受体BSA相互作用模型.通过区段-区段动力学法(Plug-plug kinetic,PPK),HD法(Hummel-Dreyer,HD),前沿分析法(Frontal analysis,FA)和空峰法(Vacant peak,VP)测定DMP与BSA的相互作用,分别运用Scatchard方程,Klotz方程和非线性方程(Non-linear regression)等理论方法获取两者的相互作用参数,进而分析理论模型适用度.结果表明,PPK法、HD法与FA法都适用于DMP-BSA体系相互作用的测定,HD法最优.模型适用度分析得出非线性回归方程为最适合的理论模型.相互作用参数测试表明DMP-BSA只有单一类型的结合位点且结合强度适中,DMP-BSA分子水平的测定结果可为DMP毒理机制的深入研究提供有益参考.

English Abstract

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