Probing the Interaction of Trans-resveratrol with Bovine Serum Albumin: A Fluorescence Quenching Study with Tachiya Model
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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 (K a) 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.
KeywordsBovine serum albumin Fluorescence spectroscopy Interaction Trans-resveratrol Tachiya model
The authors are grateful for financial supported by National Natural Science Foundation of China (grant No. 20776162 and 20775092).
- 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
- 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
- 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.Förster T (1965) In: Sinanoglu O (ed) Modern quantum chemistry. vol. 3. Academic, New York, pp 93–137Google Scholar
- 23.Timaseff SN (1972) Proteins of biological fluids. Pergamon, Oxford, pp 511–519, 45Google Scholar