Skip to main content
Log in

Spectroscopic Studies on Binding of Lotus Seedpod Oligomeric Procyanidins to Bovine Serum Albumin

  • Published:
Journal of Applied Spectroscopy Aims and scope

The binding of lotus seedpod oligomeric procyanidins (LSOPC) and catechin (a major constituent unit of LSOPC) to bovine serum albumin (BSA) was studied by a fluorescence quenching technique. The results revealed that LSOPC could strongly quench the intrinsic fluorescence of BSA through a static quenching procedure, but catechin could not. The Stern–Volmer quenching constant, K SV, and corresponding thermodynamic parameters, ΔG 0, ΔH 0 and ΔS 0, were calculated. The results of synchronous fluorescence and circular dichroism studies showed that LSOPC could cause a conformational change in BSA. In addition, glucose and metal ions could affect the interaction between LSOPC and BSA.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. J. Flarakos, K. L. Morand, P. Vouros, Anal. Chem., 77, 1345–1353 (2005).

    Article  Google Scholar 

  2. D. C. Carter, J. X. Ho, Adv. Protein Chem., 45, 153–203 (1994).

    Article  Google Scholar 

  3. A. Zhang, L. Jia, Spectrosc. Lett., 39, 285–298 (2006).

    Article  ADS  Google Scholar 

  4. K. F. Brown, M. J. Crooks, Biochem. Pharmacol., 25, 1175–1178 (1976).

    Article  Google Scholar 

  5. S. Ashoka, J. Seetharamappa, P. B. Kandagal, J. Lumin., 121, 179–186 (2006).

    Article  Google Scholar 

  6. X. L. Han, P. Mei, Y. Liu, Spectrochim. Acta, A, 74, 781–787 (2009).

    Article  ADS  Google Scholar 

  7. R. B. Gregory, M. Gaugoda, R. K. Gilpin, W. Su, Biopolymers, 33, 1871–1876 (1993).

    Article  Google Scholar 

  8. V. Bhakuni, C. M. Gupta, FEBS Lett., 205, 347–350 (1986).

    Article  Google Scholar 

  9. E. Shechter, E. R. Blout, Proc. Natl. Acad. Sci. USA, 51, 670—675 (1964).

    Google Scholar 

  10. W. Lindner, J. Chromatogr. B, 677, 1–28 (1996).

    Article  Google Scholar 

  11. D. E. Epps, T. J. Raub, V. Caiolfa, J. Pharm. Pharmacol., 51, 41–48 (1998).

    Article  Google Scholar 

  12. T. F. Jiang, Y. H. Wang, Z. H. Lv, J. Pharm. Biomed. Anal., 43, 854–858 (2007).

    Article  Google Scholar 

  13. M. Leopoldini, N. Russo, M. Toscano, J. Agr. Food Chem., 55, 7944–7949 (2007).

    Article  Google Scholar 

  14. H. Qu, Y. Ma, K. Yu, J. Pharm. Biomed. Anal., 43, 66–72 (2007).

    Article  Google Scholar 

  15. Y. S. Gong, Y. Tang, J. S. Xiong, B. J. Xie, Acta Nutrimenta Sinica, 28, 318–321 (2010).

    Google Scholar 

  16. D. W. Boulton, U. K. Walle, T. Walle, J. Pharm. Pharmacol., 50, 243–249 (1998).

    Article  Google Scholar 

  17. J. Liu, J. Tian, W. He, J. Pharm. Biomed. Anal., 35, 671–677 (2004).

    Article  Google Scholar 

  18. Y. Q. Wang, H. M. Zhang, G. C. Zhang, J. Lumin., 126, 211–218 (2007).

    Article  Google Scholar 

  19. S. Bi, L. Ding, Y. Tian, J. Mol. Struct., 703, 37–45 (2004).

    Article  ADS  Google Scholar 

  20. W. G. Cao, Q. C. Jiao, Y. Fu, Spectrosc. Lett., 36, 197–209 (2003).

    Article  ADS  Google Scholar 

  21. R. K. Nanda, N. Sarkar, R. Banerjee, J. Photochem. Photobiol. A, 192, 152–158 (2007).

    Article  Google Scholar 

  22. T. Yuan, A. M. Weljie, H. J. Vogel, Biochemistry, 37, 3187–3195 (1998).

    Article  Google Scholar 

  23. J. Chen, X. Y. Jiang, X. Q. Chen, J. Mol. Struct., 876, 121–126 (2008).

    Article  ADS  Google Scholar 

  24. Y. Z. Zhang, B. Zhou, X. P. Zhang, J. Hazard. Mater., 163, 1345–1352 (2009).

    Article  Google Scholar 

  25. G. Z. Chen, X. Z. Huang, J. G. Xu, Z. Z. Zheng, Z. B. Wang, Beijing Science Press, 2–112 (1990).

  26. J. R. Lakowicz, G. Weber, Biochemistry, 12, 4161–4170 (1973).

    Article  Google Scholar 

  27. S. Bi, D. Song, Y. Tian, Spectrochim. Acta, A, 61, 629–636 (2005).

    Article  ADS  Google Scholar 

  28. D. Leckband, Annu. Rev. Biophys. Biom., 29, 1–26 (2000).

    Article  Google Scholar 

  29. P. D. Ross, Biochemistry, 20, 3096–3102 (1981).

    Article  Google Scholar 

  30. G. Sudlow, D. J. Birkett, D. N. Wade, Mol. Pharmacol., 12, 1052–1061 (1976).

    Google Scholar 

  31. Q. Zhang, Y. Ni, S. Kokot, Spectrosc. Lett., 45, 85–92 (2012).

    Article  ADS  Google Scholar 

  32. Z. H. Wang, Z. D. Sun, B. J. Xie, Food Sci., 32, 77–82 (2011).

    Google Scholar 

  33. H. Liang, Y. Q. Zhou, P. W. Shen, Chin. Sci. Bull., 39, 1452–1457 (1994).

    Google Scholar 

  34. H. Gao, L. Lei, J. Liu, Q. Kong, X. Chen, Z. Hu, J. Photochem. Photobiol. A, 167, 213–221 (2004).

    Article  Google Scholar 

  35. U. Katrahalli, S. Jaldappagari, S. S. Kalanur, J. Lumin., 130, 211–216 (2010).

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Zh. Sun.

Additional information

Published in Zhurnal Prikladnoi Spektroskopii, Vol. 80, No. 6, pp. 893–900, November–December, 2013.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wu, Q., Li, S., Fu, X. et al. Spectroscopic Studies on Binding of Lotus Seedpod Oligomeric Procyanidins to Bovine Serum Albumin. J Appl Spectrosc 80, 884–892 (2014). https://doi.org/10.1007/s10812-014-9860-6

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10812-014-9860-6

Keywords

Navigation