Abstract
The binding reaction of oxymatrine (OMT) with bovine serum albumin (BSA) was studied by the methods of isothermal titration calorimetry, fluorescence, and circular dichroism (CD) spectroscopy. The thermodynamic results indicated that there were two classes of binding sites on the BSA molecule for OMT molecule. When the drug molecule binding to the first class of sites, the standard changes of enthalpy (ΔH 1°) and entropy (ΔS 1°) were (−1.07 ± 0.50) kJ/mol and (98.3 ± 0.50) J/mol/K, respectively. The possible largest number of binding site (N 1) was (10.0 ± 0.20). This type of binding was an enthalpy–entropy synergically driven process. On the second class of binding sites, the standard changes of enthalpy (ΔH 2°) and entropy (ΔS 2°) were (1.91 ± 0.03) kJ/mol and (79.8 ± 0.40) J/mol/K, respectively. The possible largest number of binding site (N 2) was (25.0 ± 0.30). This type of binding was entropy driven process. The intrinsic fluorescence of BSA was slightly quenched by the formation of BSA–OMT complex. The CD spectra experiment showed that the α-helix contents of BSA decreased. These revealed that the microenvironment and conformation of BSA were changed in the binding reaction.
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References
Aki H, Goto M, Kai M, Yamamoto M (1999) Competitive binding of drugs to the multiple binding sites on human serum albumin: a calorimetric study. J Therm Anal Calorim 57:361–370. doi:10.1023/A:1010154211244
Anbazhagan V, Renganathan R (2008) Study on the binding of 2,3-diazabicyclo [2.2.2] oct-2-ene with bovine serum albumin by fluorescence spectroscopy. Luminescence 128:1454–1458. doi:10.1016/j.jlumin.2008.02.004
Bai G, Wang Y, Yan H (2002) Therodynamics of interaction between cationic gemini surfactants and hydrophobically bodified polymers in aqueous solutions. J Phys Chem B 106:2153–2159. doi:10.1021/jp0123839
Boyer C, Bulmus V, Liu JQ, Davis TP, Stenzel MH, Barner-Kowollik C (2007) Well-defined protein–polymer conjugates via in situ RAFT polymerization. J Am Chem Soc 129:7145–7154. doi:10.1021/ja070956a
Cheng ZJ, Zhang YT (2008) Fluorometric investigation on the interaction of oleanolic acid with bovine serum albumin. J Mol Struct 879:81–87. doi:10.1016/j.molstruc.2007.08.020
Cheng YQ, Chen HL, Li YQ, Chen XG, Hu ZD (2004) Separation and determination of aloperine, sophoridine, matrine and oxymatrine by combination of flow injection with microfluidic capillary electrophoresis. Talanta 63:491–496. doi:10.1016/j.talanta.2003.11.027
De S, Girigoswami A, Das S (2005) Fluorescence probing of albumin–surfactant interaction. J Colloid Interface Sci 285:562–573. doi:10.1016/j.jcis.2004.12.022
Ding YH, Shu Y, Ge LL, Guo R (2007) The effect of sodium dodecyl sulfate on the conformation of bovine serum albumin. Colloid Surf A 298:163–169. doi:10.1016/j.colsurfa.2006.10.058
Dong Y, Xi H, Yu Y, Wang Q, Jiang K, Li L (2002) Effects of serum levels of T helper cell 1 and 2 cytokines and the expression of S gene in hepatitis B virus S gene transgenic mice: a study of the anti-hepatitis B virus mechanism of oxymatrine. J Gastroenterol Hepatol 17:1299–1306. doi:10.1046/j.1440-1746.2002.02885.x
Gharagozlou M, Boghaei DM (2008) Interaction of water-soluble amino acid Schiff base complexes with bovine serum albumin: fluorescence and circular dichroism studies. Spectrochim Acta A 71:1617–1622. doi:10.1016/j.saa.2008.06.027
Jong TT, Lee MR, Chiang YC, Chiang ST (2006) Using LC/MS/MS to determine matrine, oxymatrine, ferulic acid, mangiferin, and glycyrrhizin in the Chinese medicinal preparations Shiau-feng-saan and Dang-guei-nian-tong-tang. J Pharm Biomed 40:472–477. doi:10.1016/j.jpba.2005.07.036
Kelarakis A, Castelletto V, Krysmann MJ, Havredaki V, Viras K, Hamley IW (2008) Interactions of bovine serum albumin with ethylene oxide/butylene oxide copolymers in aqueous solution. Biomacromolecules 9:1366–1371. doi:10.1021/bm800046m
Ku YR, Chang LY, Lin JH, Ho LK (2002) Determination of matrine and oxymatrine in Sophora subprostata by CE. J Pharm Biomed 28:1005–1010. doi:10.1016/S0731-7085(02)00050-X
Lin LN, Mason AB, Woodworth RC, Brandts JF (1991) Calorimetric studies of the binding of ferric ions to ovotransferrin and interactions between binding sites. Biochemistry 30:11660–11669. doi:10.1021/bi00114a008
Luo L, He JX, Zhu XJ, Jiang CQ (2008) Study of the interaction between nucleic acids and the daunoblastina aluminum (III) complex. Med Chem Res 17:42–50. doi:10.1007/s00044-008-9091-6
Monti S, Manet I, Manoli F, Capobianco ML, Marconi G (2008) Gaining an insight into the photoreactivity of a drug in a protein environment: a case study on nalidixic acid and serum albumin. J Phys Chem B 112:5742–5754. doi:10.1021/jp711261n
Moosavi-Movahedi AA, Bordbar AK, Taleshi AA, Naderimanesh HM, Ghadam P (1996) Mechanism of denaturation of bovine serum albumin by dodecyl trimethylammonium bromide. J Biochem Cell Biol 28:991–998. doi:10.1016/1357-2725(96)00044-1
Nazari K, Gholami N, Moosavi-Movahedi AA (2007) Stability of DNA upon interaction with dimethyltin dichloride. Med Chem Res 16:238–257. doi:10.1007/s00044-007-9028-5
Nielsen AD, Borch K, Westh P (2000) Thermochemistry of the specific binding of C12 surfactants to bovine serum albumin. Biochim Biophys Acta 1479:321–331
Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096–3102. doi:10.1021/bi00514a017
Song GB, Luo Q, Qin J, Wang L, Shi YS, Sun CX (2006) Effects of oxymatrine on proliferation and apoptosis in human hepatoma cells. Colloid Surf B 48:1–5. doi:10.1016/j.colsurfb.2005.12.012
Torresa J, Kremera C, Pardob H, Suescunb L, Mombrúb A, Castiglionic J, Domŕnguezd S, Mederosd A, Kremera E (2003) Preparation and crystal structure of new samarium complexes with glutamic acid. J Mol Struct 660:99–106. doi:10.1016/j.molstruc.2003.08.003
Wang SJ, Wang GJ, Li XT, Sun JG, Ma RL, Sheng LS (2005) Simultaneous determination of oxymatrine and its active metabolite matrine in dog plasma by liquid chromatography–mass spectrometry and its application to pharmacokinetic studies. J Chromatogr B 817:319–325. doi:10.1016/j.jchromb.2005.01.003
Wang X, Zhang W, Fan LY, Hao B, Ma AN, Cao CX, Wang YX (2007) Sensitive quantitative determination of oxymatrine and matrine in rat plasma by capillary electrophoresis with stacking induced by moving reaction boundary. Anal Chim Acta 594:290–296. doi:10.1016/j.aca.2007.05.024
Wang N, Ye L, Yan FF, Xu R (2008) Spectroscopic studies on the interaction of azelnidipine with bovine serum albumin. Int J Pharm 351:55–60. doi:10.1016/j.ijpharm.2007.09.016
Wiseman T, Wiliston S, Brandts JF, Lin LN (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179:131–137. doi:10.1016/0003-2697(89)90213-3
Wu XL, Hang TJ, Shen JP, Zhang YD (2006) Determination and pharmacokinetic study of oxymatrine and its metabolite matrine in human plasma by liquid chromatography tandem mass spectrometry. J Pharm Biomed 41:918–924. doi:10.1016/j.jpba.2006.01.029
Xu GL, Yao L, Rao SY, Gong ZN, Zhang SQ, Yu SQ (2005) Attenuation of acute lung injury in mice by oxymatrine is associated with inhibition of phosphorylated p38 mitogen-activated protein kinase. J Ethnopharmacol 98:177–183. doi:10.1016/j.jep.2005.01.026
Yu ZL, Li DJ, Ji BM, Chen JJ (2008) Characterization of the binding of nevadensin to bovine serum albumin by optical spectroscopic technique. J Mol Struct 889:422–428. doi:10.1016/j.molstruc.2008.03.013
Zhang YZ, Dai J, Zhang XP, Yang X, Liu Y (2008a) Studies of the interaction between Sudan I and bovine serum albumin by spectroscopic methods. J Mol Struct 888:152–159. doi:10.1016/j.molstruc.2007.11.043
Zhang L, Liu WT, Zhang RW, Wang ZW, Shen ZD, Chen XH, Bi KS (2008b) Pharmacokinetic study of matrine, oxymatrine and oxysophocarpine in rat plasma after oral administration of Sophora flavescens Ait. extract by liquid chromatography tandem mass spectrometry. J Pharm Biomed 47:892–898. doi:10.1016/j.jpba.2008.03.019
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This work was supported by the National Natural Science Foundation of China (No. 20673050) and was partially supported by Shandong Tai-Shan Scholar Research Fund.
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Xu, X., Zhu, L., Sun, X. et al. Study on the interaction of oxymatrine with bovine serum albumin. Med Chem Res 20, 746–751 (2011). https://doi.org/10.1007/s00044-010-9382-6
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DOI: https://doi.org/10.1007/s00044-010-9382-6