Issue

Vol. 25 No. 8 (2013): Vol 25 Issue 8

Copyright (c) 2013 AJC

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Study on the Interaction Between Salvianolic Acid B and Bovine Serum Albumin by Spectroscopic Techniques

https://doi.org/10.14233/ajchem.2013.14024
Qing Zhu
Qilu Hospital of Shangdong University, 107 West of Wenhua Street, Jinan, Shandong 250012, P.R. China
Mei Wang
Shandong Normal University, 88 East of Wenhua Street, Jinan, Shandong 250014, P.R. China
Feng Liu
Shandong Analysis and Test Center, Shandong Academy of Sciences, 19 Keyuan Street, Jinan, Shandong 250014, P.R. China
Xiao Wang
Shandong Analysis and Test Center, Shandong Academy of Sciences, 19 Keyuan Street, Jinan, Shandong 250014, P.R. China

Corresponding Author(s) : Xiao Wang

wangxiao2008@yahoo.cn

Asian Journal of Chemistry, Vol. 25 No. 8 (2013): Vol 25 Issue 8

Abstract

Under simulated physiological conditions, the interaction between salvianolic acid B and bovine serum albumin was investigated using fluorescence spectroscopy, synchronous fluorescence spectroscopy, circular dichroism and ultraviolet spectroscopy at different conditions. As a result, the binding constant (K), the numbers of binding sites (n), the binding distance (r) and the thermodynamic parameters enthalpy change (DHº), the entropy change (DSº), Gibbs free energy change (DGº), are calculated in a simulated human body conditions. The conformation of bovine serum albumin changed in the presence of salvianolic acid B on circular dichroism and synchronous fluorescence spectroscopy. The results show that the static quenching and non-radiative energy transfer lead to the fluorescence quenching of bovine serum albumin and salvianolic acid B-bovine serum albumin system is a spontaneous reaction, the main electrostatic force is hydrophobic effect. In addition, the addition of external common metal ions Cu2+ and K+ decreased the binding constant between salvianolic acid B and bovine serum albumin.

Keywords

Salvianolic acid B Bovine serum albumin Fluorescence quenching Interaction
Zhu, Q., Wang, M., Liu, F., & Wang, X. (2013). Study on the Interaction Between Salvianolic Acid B and Bovine Serum Albumin by Spectroscopic Techniques. Asian Journal of Chemistry, 25(8), 4475–4480. https://doi.org/10.14233/ajchem.2013.14024
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. Pharmacopoeia Commission of the People's Republic of China. Pharmacopoeia of the People's Republic of China. Beijing: Chinese MedicoPharmaceutical Sciences and Technology Publishing House (2010).
  2. L. Zhou, Z. Zuo and M.S. Chow, J. Clin. Pharmacol., 45, 1345 (2005).
  3. H.L. Wu, Y.H. Li, Y.H. Lin, R. Wang, Y.B. Li, L. Tie, Q.L. Song, D.A. Guo, H.M. Yu and X.J. Li, Cardiovasc. Res., 81, 148 (2009).
  4. Y.H. Chen, G.H. Du and J.T. Zhang, Acta Pharmacol. Sin., 21, 463 (2000).
  5. M.K. Tang, D.C. Ren, J.T. Zhang and G.H. Du, J. Phytomed., 9, 405 (2002).
  6. L. Trnková, I. Boušová, V. Stanková and J. Dršata, J. Mol. Struct., 985, 243 (2011).
  7. T. Peters, All About Albumin: Biochemistry, Genetics and Medical Applications, Academic Press, San Diego (CA), Ch. 2 and 3 (1996).
  8. D.C. Carter and J.X. Ho, Adv. Protein Chem., 45, 153 (1994).
  9. J. Seetharamappa and B.P. Kamat, Chem. Pharm. Bull., 52, 1053 (2004).
  10. B. Pal, P.K. Bajpai and T.S. Basu Baul, Spectrochim. Acta A, 56, 2453 (2000).
  11. H. Xu, S.L. Gao, J.B. Lv, Q.W. Liu, Y. Zuo and X. Wang, J. Mol. Struct., 919, 334 (2009).
  12. F. Wang, W. Huang, B. Tang and X.J. Liu, Chin. J. Anal. Chem., 34, s239 (2006).
  13. G.W. Zhang, A.P. Wang, T. Jiang and Q.M. Que, Chin. J. Anal. Lab., 27, 1 (2008).
  14. M. He, Z.N. Xia, Y.G. Yin and Z. Liu, Chin. J. Modern Appl. Pharm., 21 (2004).
  15. J.Q. Tong, H.X. Zhang, H.M. Yang and P. Mei, J. Mol. Biol. Rep., 37, 1741 (2010).
  16. G.Z. Chen, Fluorescence Analysis, Science Press, Beijing, p. 122 (1990).
  17. D.M. Zha, S. Li, Y.F. Yang, C.Q. Tu and H. Liang, Spectrosc. Spectr. Anal., 19, 21 (1999).
  18. W.Y. He, Y. Li, J.H. Tang, F. Luan, J. Jin and Z.D. Hu, J. Biol. Macromol., 39, 165 (2006).
  19. T. Förster and O. Sinanoglu, Modern Quantum Chem.,Academic Press, New York, Vol. 3, pp. 93-137 (1966).
  20. 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).
  21. Z.C. Shang, P.G. Yi, Q.S. Yu and R.S. Lin, Acta Phys. Chim. Sin., 17, 48 (2001).
  22. H. Lin, J.F. Lan, M. Guan, F.L. Sheng and H.X. Zhang, Spectrochim. Acta A, 73, 936 (2009).
  23. Z.L. Yu, D.J. Li, B.M. Ji and J.J. Chen, J. Mol. Struct., 889, 422 (2008).
  24. G.K. Wu, C.N. Yan and Y. Liu, Guang Pu Xue Yu Guang Pu Fen Xi, 28, 2139 (2008).
  25. K. Yamasaki, T. Maruyama, A. Takadata, A. Suenaga, U. Kragh-Hanse and M. Otagiri, J. Pharm. Sci., 93, 3004 (2004).
  26. H. Yang, Z.Q. Wang, Y.C. Wang and K.Y. Ni, Chin. J. Spectrosc. Lab., 25, 284 (2008).
  27. J. Gonzalez-Jimenez, H. Jacquotte and I. Cayre, Chem. Biol. Interact., 84, 221 (1992).
  28. P.D. Ross and S. Subramanian, Biochemisty, 20, 3096 (1981).
  29. G.Z. Chen, X.Z. Huang, J.J. Xu and Z.Z. Zheng, Fluorescence Analysis, M. Beijing: Science Press, pp. 201-213 (1990).
  30. A. Varlan and M. Hillebrand, Molecules, 15, 3095 (2010).
  31. H. Liang, H. Jin, Q.T. Chu, M. Zhang, Y.Q. Zhou and P.W. Shen, J. Inorg. Biochem., 85, 167 (2001).
  32. P.J. Sadler, A. Tucker and J.H. Viles, Eur. J. Med. Chem., 220, 193 (1994).
  33. W. Bal, J. Christodoulou, P.J. Sadler and A. Tucker, J. Inorg. Biochem., 70, 33 (1998).
  34. N. Wang, L. Ye, B.Q. Zhao and J.X. Yu, Braz. J. Med. Biol. Res., 41, 589 (2008).
  35. G.W. Zhang, Q.M. Que and J.H. Pan, Guang Pu Xue Yu Guang Pu Fen Xi, 27, 1784 (2007).
Read More
Author biographies is not available.
Download
PDF
Statistic
Read Counter : 0 Download : 0