Journal of Fluorescence

, Volume 18, Issue 3–4, pp 671–678 | Cite as

Probing the Interaction of Trans-resveratrol with Bovine Serum Albumin: A Fluorescence Quenching Study with Tachiya Model

Original Paper

Abstract

The interaction of trans-resveratrol (TRES) and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) with Tachiya model. The binding number maximum of TRES was determined to be 8.86 at 293.15 K, 23.42 at 303.15 K and 33.94 at 313.15 K and the binding mechanism analyzed in detail. The apparent binding constants (Ka) between TRES and BSA were 5.02 × 104 (293.15 K), 8.89 × 104 (303.15 K) and 1.60 × 105 L mol−1 (313.15 K), and the binding distances (r) between TRES and BSA were 2.44, 3.01, and 3.38 nm at 293.15, 303.15, and 313.15 K, respectively. The addition of TRES to BSA solution leads to the enhancement in RLS intensity, exhibiting the formation of the aggregate in solution. The negative entropy change and enthalpy change indicated that the interaction of TRES and BSA was driven mainly by van der Waals interactions and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative.

Keywords

Bovine serum albumin Fluorescence spectroscopy Interaction Trans-resveratrol Tachiya model 

Notes

Acknowledgments

The authors are grateful for financial supported by National Natural Science Foundation of China (grant No. 20776162 and 20775092).

References

  1. 1.
    Xiang GH, Tong CL, Lin HZ (2007) Nitroaniline Isomers Interaction with Bovine Serum Albumin and Toxicological Implications. J Fluoresc 17:512–521PubMedCrossRefGoogle Scholar
  2. 2.
    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 55:6726–6735PubMedCrossRefGoogle Scholar
  3. 3.
    Xiao JB, Shi J, Cao H, Wu SD, Ren FL, Xu M (2007) Analysis of binding interaction between puerarin and bovine serum albumin by multi-spectroscopic method. J Pharmaceut Biomed 45:609–615CrossRefGoogle Scholar
  4. 4.
    Ran D, Wu X, Zheng J, Yang J, Zhou H, Zhang M, Tang Y (2007) Study on the interaction between florasulam and bovine serum albumin. J Fluoresc 17:721–726PubMedCrossRefGoogle Scholar
  5. 5.
    Cui FL, Wang JL, Cui YR, Li JP (2006) Fluorescent investigation of the interactions between N-(p-chlorophenyl)-N′-(1-naphthyl) thiourea and serum albumin: synchronous fluorescence determination of serum albumin. Anal Chim Acta 571:175–183PubMedCrossRefGoogle Scholar
  6. 6.
    Shang L, Jiang X, Dong S (2006) In vitro study on the binding of neutral red to bovine serum albumin by molecular spectroscopy. J Photochem Photobiol A 184:93–97CrossRefGoogle Scholar
  7. 7.
    Bose B, Dube A (2006) Interaction of Chlorin p6 with bovine serum albumin and photodynamic oxidation of protein. J Photochem Photobiol B 85:49–55PubMedCrossRefGoogle Scholar
  8. 8.
    Zhou N, Liang YZ, Wang P (2007) 18b-Glycyrrhetinic acid interaction with bovine serum albumin. J Photochem Photobiol A 185:271–276CrossRefGoogle Scholar
  9. 9.
    Hu YJ, Liu Y, Zhao RM, Dong JX, Qu SS (2006) Spectroscopic studies on the interaction between methylene blue and bovine serum albumin. J Photochem Photobiol A 179:324–329CrossRefGoogle Scholar
  10. 10.
    Wang YP, Wei YL, Dong C (2006) Study on the interaction of 3,3-bis(4-hydroxy-1-naphthyl)-phthalide with bovine serum albumin by fluorescence spectroscopy. J Photochem Photobiol A 177:6–11CrossRefGoogle Scholar
  11. 11.
    Cao H, Xiao JB, Xu M (2006) Evaluation of new selective molecularly imprinted polymers for the extraction of reveratrol from Polygonum cuspidatum. Macromolecular Res 14:324–330Google Scholar
  12. 12.
    Maron DJ (2004) Flavonoids for reduction of atherosclerotic risk. Curr Atheroscler Rep 6:73–78PubMedCrossRefGoogle Scholar
  13. 13.
    Baur JA, Sinclair DA (2006) Therapeutic potential of resveratrol: the in vivo evidence. Nat Rev Drug Discov 5:493–506PubMedCrossRefGoogle Scholar
  14. 14.
    Das S, Tosaki A, Bagchi D, Maulik N, Das DK (2006) Potentiation of a survival signal in the ischemic heart by resveratrol through p38 mitogen-activated protein kinase/mitogen- and stress-activated protein kinase 1/cAMP response element-binding protein signaling. J Pharmacol Exp Ther 317:980–988PubMedCrossRefGoogle Scholar
  15. 15.
    Fukuda S, Kaga S, Zhan L, Bagchi D, Das DK, Bertelli A (2006) Resveratrol ameliorates myocardial damage by inducing vascular endothelial growth fantorangiogenesis and tyrosine kinase receptor Flk-1. Cell Biochem Biophys 44:43–49PubMedCrossRefGoogle Scholar
  16. 16.
    Raval AP, Dave KR, Perez-Pinzon MA (2006) Resveratrol mimics ischemic preconditioning in the brain. J Cereb Blood Flow Metab 26:1141–1147PubMedGoogle Scholar
  17. 17.
    Kumar A, Kaundal RK, Iyer S, Sharma SS (2007) Effects of resveratrol on nerve functions, oxidative stress and DNA fragmentation in experimental diabetic neuropathy. Life Sci 80:1236–1244PubMedCrossRefGoogle Scholar
  18. 18.
    Tachiya M (1982) Kinetics of quenching of luminescent probes in micellar systems II. J Chem Phys 76:340–348CrossRefGoogle Scholar
  19. 19.
    Horrocks WD, Collier WE (1981) Lanthanide ion luminescence probes. Measurement of distance between intrinsic protein fluorophores and bound metal ions: quantitation of energy transfer between tryptophan and terbium(III) or europium(III) in the calcium-binding protein parvalbumin. J Am Chem Soc 103:2856–2862CrossRefGoogle Scholar
  20. 20.
    Förster T (1965) In: Sinanoglu O (ed) Modern quantum chemistry. vol. 3. Academic, New York, pp 93–137Google Scholar
  21. 21.
    Wang C, Wu QH, Wang Z, Zhao J (2006) Study of the interaction of carbamazepine with bovine serum albumin by fluorescence quenching method. Anal Sci 22:435–438PubMedCrossRefGoogle Scholar
  22. 22.
    Ross PD, Subramanian S (1981) Thermodynamics of protein association reaction: forces contribution to stability. Biochemistry 20:3096–3102PubMedCrossRefGoogle Scholar
  23. 23.
    Timaseff SN (1972) Proteins of biological fluids. Pergamon, Oxford, pp 511–519, 45Google Scholar
  24. 24.
    Liu ZD, Huang CZ, Li YF, Long YF (2006) Enhanced plasmon resonance light scattering signals of colloidal gold resulted from its interactions with organic small molecules using captopril as an example. Anal Chim Acta 577:244–249PubMedCrossRefGoogle Scholar
  25. 25.
    Xiao JB, Yang CS, Ren FL, Jiang XY, Xu M (2007) Rapid determination of ciprofloxacin lactate in drugs by Rayleigh light scattering technique. Meas Sci Technol 18:859–866CrossRefGoogle Scholar
  26. 26.
    Xiao JB, Chen JW, Ren FL, Yang CS, Xu M (2007) Use of 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl tetrazolium bromide for rapid detection of methicillin-resistant Staphylococcus aureus by resonance light scattering. Anal Chim Acta 589:186–191PubMedCrossRefGoogle Scholar
  27. 27.
    Chen JW, Yang CS, Ren FL, Xiao JB, Xu M (2007) Highly sensitive determination of chloride ion in serum using Rayleigh light scattering technique. Meas Sci Technol 18:2043–2047CrossRefGoogle Scholar
  28. 28.
    Chen ZG, Liu JB, Han YL, Zhu L (2006) A novel histidine assay using tetraphenylporphyrin manganese (III) chloride as a molecular recognition probe by resonance light scattering technique. Anal Chim Acta 570:109–115CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2008

Authors and Affiliations

  1. 1.College of Chemistry and Chemical EngineeringCentral South UniversityChangshaPeople’s Republic of China
  2. 2.Department of Nutrition, Faculty of Health and WelfareOkayama Prefectural UniversitySojaJapan
  3. 3.Institute of Applied Radiation ChemistryTechnical University of LodzLodzPoland
  4. 4.National Institute of Advanced Industrial Science and Technology (AIST)TsukubaJapan

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