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Copyright (c) 2014 Rendong Ji1, Zhimin Zhao1, Xingyue Zhu1, Menglan Chen1, Xiaoyan Wang1
This work is licensed under a Creative Commons Attribution 4.0 International License.
Spectroscopic Studies on Interaction Between Enalapril Maleate and Bovine Serum Albumin
Corresponding Author(s) : Rendong Ji1
Asian Journal of Chemistry,
Vol. 26 No. 24 (2014)
Abstract
The interaction between enalapril maleate and bovine serum albumin was investigated by fluorescence and absorption spectroscopy under simulative physiological conditions. It was revealed that the quenching mechanism of bovine serum albumin by enalapril maleate is static quenching mechanism. The binding sites number and binding constant were obtained at different temperature. The thermodynamic parameters were abtained according to van’t Hoff equation and the result indicates that the interaction between enalapril maleate and bovine serum albumin is driven mainly by electrostatic forces. The distance between enalapril maleate and the protein was calculated to be about 3.78 nm according to the theory of Föster energy transfer.
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References
X.M. He and D.C. Carter, Nature, 358, 209 (1992).
D.D. Carter and J.X. Ho, Adv. Protein Chem., 45, 153 (1994).
L. Trnková, I. Boušová, V. Staòková and J. Dršata, J. Mol. Struct., 985, 243 (2011).
X.Y. Yu, R.H. Liu, F.X. Yang, D.H. Ji, X.F. Li, J. Chen, H.W. Huang and P.G. Yi, J. Mol. Struct., 985, 407 (2011).
T.T. Xu, Q. Wu, X.W. Lv, F. Yu and Y. Tan, Chinese J. Exper. Tradit. Med. Formulae, 19, 291 (2013).
T. Arafat, R. Awad, M. Hamad, R. Azzam, A. Al-Nasan, A. Jehanli and K. Matalka, J. Clin. Pharm. Ther., 30, 319 (2005).
R.L.O. Rezende, M.I.R.M. Santoro and J.R. Matos, J. Therm. Anal. Calorim., 93, 881 (2008).
F. Wedian and A. Lataifeh, Int. J. Chem., 5, 29 (2013).
T.H. Wang, Z.M. Zhao, L. Zhang and L. Ji, J. Mol. Struct., 937, 65 (2009).
M. Pistolozzi, C. Franchini, F. Corbo, M. Muraglia, M. De Giorgi, G. Felix and C. Bertucci, J. Pharmaceut. Biomed., 53, 179 (2010).
R. Mallik, M.J. Yoo, S. Chen and D.S. Hage, J. Chromatogr. B, 876, 69 (2008).
M.S. Chernovyants, A.O. Dolinkin, A.V. Chernyshev, E.V. Khohlov and E.G. Golovanova, J. Pharm. Sci., 99, 1567 (2010).
L. Ding, X.X. Zhang, W.B. Chang, W. Lin and M. Yang, Chinese J. Chromatogr. A, 22, 624 (2004).
P.N. Naik, S.A. Chimatadar and S.T. Nandibewoor, J. Photochem. Photobiol. B, 100, 147 (2010).
T.H. Wang, Z.M. Zhao, B.Z. Wei, L. Zhang and L. Ji, J. Mol. Struct., 970, 128 (2010).
B. Hemmateenejad and S. Yousefinejad, J. Mol. Struct., 1037, 317 (2013).
J.R. Lakowicz and G. Weber, Biochemistry, 12, 4171 (1973).
T.H. Wang, Z.Z. Zhao, J. Hua and J.H. Zhang, Indian J. Biochem. Biophys., 48, 388 (2011).
S. Bi, D. Song, Y. Kan, D. Xu, Y. Tian, X. Zhou and H. Zhang, Spectrochim. Acta A, 62, 203 (2005).
P.D. Ross and S. Subramanian, Biochemistry, 20, 3096 (1981).
L.A. Sklar, B.S. Hudson and R.D. Simoni, Biochemistry, 16, 5100 (1977).
C.D. Kanakis, P.A. Tarantilis, M.G. Polissiou, S. Diamantoglou and H.A. Tajmir-Riahi, J. Mol. Struct., 798, 69 (2006).
S. Kasai, T. Horie, T. Mizuma and S. Awazu, J. Pharm. Sci., 76, 387 (1987).
X.F. Liu, Y.M. Xia, Y. Fang, L.L. Liu and L. Zou, Chem. J. Chin. Univ., 25, 2099 (2004).