Skip to main content
Log in

Binding Citrus flavanones to human serum albumin: effect of structure on affinity

  • Published:
Molecular Biology Reports Aims and scope Submit manuscript

Abstract

Much of the bioactivities of Citrus flavanones significantly appear to impact blood and microvascular endothelial cells. It is essential to investigate the interaction between Citrus flavanones and serum albumin to verify the effect of flavanone structures on the distribution and transportation in blood. The interactions between flavonoids and proteins have attracted great interest among researchers. The work in here mainly concerns about the binding interaction between Citrus flavanones and human serum albumin (HSA) in vitro. The methoxylation of tangeretin improved the affinity for HSA by 100 times. The 2,3-double bond in conjugation with a 4-oxo group plays an important role for the affinity for HSA. The affinity of apigenin for HSA is about 10,000-times higher than that of naringenin. It was found that the hydroxylation on position 3′ of flavonol significantly improves the binding affinity for HSA. The affinity of quercetin (3′, 4′) for HSA is about 100-times higher than that of kaempferol (4′). The hydroxylation on position 3′ of flavone slightly improves the binding affinity for HSA. The affinity of luteolin for HSA is about 1.38-times higher than that of apigenin. The values of log10(Ka) are proportional to the number of binding sites (n), which confirms the method used here is suitable to study the interaction between Citrus flavanones and HSA.

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.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Ghosh D, Scheepens A (2009) Vascular action of polyphenols. Mol Nutr Food Res 53:322–331

    Article  PubMed  CAS  Google Scholar 

  2. Krafczyk N, Woyand F, Glomb MA (2009) Structure-antioxidant relationship of flavonoids from fermented rooibos. Mol Nutr Food Res 53:635–642

    Article  PubMed  CAS  Google Scholar 

  3. Sepehr E, Cooke GM, Robertson P, Gilani GS (2009) Effect of glycosidation of isoflavones on their bioavailability and pharmacokinetics in aged male rats. Mol Nutr Food Res 53:S16–S26

    Article  PubMed  Google Scholar 

  4. Ahn MR, Kunimasa K, Kumazawa S, Nakayama T, Kaji K, Uto Y, Hori H, Nagasawa H, Ohta T (2009) Correlation between antiangiogenic activity and antioxidant activity of various components from propolis. Mol Nutr Food Res 53:643–651

    Article  PubMed  CAS  Google Scholar 

  5. Tripoli E, La Guardia M, Giammanco S, Di Majo D, Giammanco M (2007) Citrus flavonoids: molecular structure, biological activity and nutritional properties: a review. Food Chem 104:466–479

    Article  CAS  Google Scholar 

  6. Abe K, Katayama H, Suzuki A, Yumioka E (1993) Biological fate of orally administered naringin and naringenin in rats. Jpn J Pharmacog 47:402–407

    CAS  Google Scholar 

  7. Choudhury R, Chowrimootoo G, Srai K, Debnam E, Rice-Evans C (1999) Interactions of the flavonoid naringenin in the gastrointestinal tract and the influence of glycosylation. Biochem Biophys Res Co 265:410–415

    Article  CAS  Google Scholar 

  8. Benavente-García O, Castillo J (2008) Update on uses and properties of Citrus flavonoids: new findings in anticancer, cardiovascular, and anti-inflammatory activity. J Agric Food Chem 56:6185–6205

    Article  PubMed  Google Scholar 

  9. Otagiri M (2005) A molecular functional study on the interactions of drugs with plasma proteins. Drug Metab Pharmacokinet 20:309–323

    Article  PubMed  CAS  Google Scholar 

  10. Bae MJ, Ishii T, Minoda K, Kawada Y, Ichikawa T, Mori T (2009) Albumin stabilizes (–)-epigallocatechin gallate in human serum: binding capacity and antioxidant property. Mol Nutr Food Res 53:709–715

    Article  PubMed  CAS  Google Scholar 

  11. Xiao JB, Chen TT, Cao H, Chen LS, Yang F (2010) Molecular property-affinity relationship of flavanoids and flavonoids for human serum albumin in vitro. Mol Nutr Food Res (in press). doi:10.1002/mnfr.201000208

  12. Xiao J, Chen X, Zhang L, Talbot SG, Li GC, Xu M (2008) Investigation the mechanism of enhanced effect of EGCG on huperzine A inhibiting acetylcholinesterase activity in rats by multi-spectroscopic method. J Agric Food Chem 56:910–915

    Article  PubMed  CAS  Google Scholar 

  13. Xiao JB, Cao H, Wang YF, Yamamoto K, Wei XL (2010) Structure-affinity relationship of flavones on binding to serum albumins: effect of hydroxyl groups on ring A. Mol Nutr Food Res 54:S253–S260

    Article  PubMed  CAS  Google Scholar 

  14. Xiao JB, Suzuki M, Jiang XY, Chen XQ, Yamamoto K, Xu M (2008) Influence of B-ring hydroxylation on interactions of flavonols with bovine serum albumin. J Agric Food Chem 56:2350–2356

    Article  PubMed  CAS  Google Scholar 

  15. Xiao JB, Cao H, Wang YF, Zhao JY, Wei XL (2009) Glycosylation of dietary flavonoids decreases the affinities for plasma protein. J Agric Food Chem 57:6642–6648

    Article  PubMed  CAS  Google Scholar 

  16. Soares S, Mateus N, Freitas V (2007) Interaction of different polyphenols with bovine serum albumin (BSA) and human salivary R-amylase (HSA) by fluorescence quenching. J Agric Food Chem 55:6726–6735

    Article  PubMed  CAS  Google Scholar 

  17. Lakowicz JR (1999) Principles of fluorescence spectroscopy, 2nd edn. Kluwer Academic/Plenum Publishers, New York

    Google Scholar 

  18. Woodman OL, Meeker WF, Boujaoude M (2005) Vasorelaxant and antioxidant activity of flavonols and flavones: structure activity relationships. J CardioVasc Pharm 46:302–309

    Article  CAS  Google Scholar 

  19. Heijnen CGM, Haenen GRMM, van Acker FAA, van der Vijgh WJF, Bast A (2001) Flavonoids as peroxynitrite scavengers: the role of the hydroxyl groups. Toxicol In Vitro 15:3–6

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgments

The authors are grateful for the financial support sponsored by Natural Science Foundation of Shanghai (10ZR1421700), “Chen Guang” project supported by Shanghai Municipal Education Commission and Shanghai Education Development Foundation (09CG46), Leading Academic Discipline Project of Shanghai Municipal Education Commission (J50401) and Innovation Program of Shanghai Municipal Education Commission (10YZ68).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Jianbo Xiao.

Additional information

Hui Cao and Longsheng Chen contributed equally to this work.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Cao, H., Chen, L. & Xiao, J. Binding Citrus flavanones to human serum albumin: effect of structure on affinity. Mol Biol Rep 38, 2257–2262 (2011). https://doi.org/10.1007/s11033-010-0356-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11033-010-0356-z

Keywords

Navigation