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

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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 (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.

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Acknowledgments

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

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Authors and Affiliations

  1. College of Chemistry and Chemical Engineering, Central South University, Changsha, 410083, People’s Republic of China

    J. B. Xiao, X. Q. Chen & X. Y. Jiang

  2. Department of Nutrition, Faculty of Health and Welfare, Okayama Prefectural University, Kuboki 111, Soja, Okayama, 719-1197, Japan

    J. B. Xiao

  3. Institute of Applied Radiation Chemistry, Technical University of Lodz, Wroblewskeigo 15, 93-590, Lodz, Poland

    M. Hilczer

  4. National Institute of Advanced Industrial Science and Technology (AIST), AIST Central 5, Tsukuba, Ibaraki, 305-8565, Japan

    M. Tachiya

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  1. J. B. Xiao
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  2. X. Q. Chen
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  3. X. Y. Jiang
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  4. M. Hilczer
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  5. M. Tachiya
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Correspondence to X. Q. Chen or M. Tachiya.

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Xiao, J.B., Chen, X.Q., Jiang, X.Y. et al. Probing the Interaction of Trans-resveratrol with Bovine Serum Albumin: A Fluorescence Quenching Study with Tachiya Model. J Fluoresc 18, 671–678 (2008). https://doi.org/10.1007/s10895-008-0346-x

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  • DOI: https://doi.org/10.1007/s10895-008-0346-x

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