Original Paper

Journal of Fluorescence

, Volume 18, Issue 3, pp 671-678

First online:

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

  • J. B. XiaoAffiliated withCollege of Chemistry and Chemical Engineering, Central South UniversityDepartment of Nutrition, Faculty of Health and Welfare, Okayama Prefectural University
  • , X. Q. ChenAffiliated withCollege of Chemistry and Chemical Engineering, Central South University Email author 
  • , X. Y. JiangAffiliated withCollege of Chemistry and Chemical Engineering, Central South University
  • , M. HilczerAffiliated withInstitute of Applied Radiation Chemistry, Technical University of Lodz
  • , M. TachiyaAffiliated withNational Institute of Advanced Industrial Science and Technology (AIST) Email author 

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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.


Bovine serum albumin Fluorescence spectroscopy Interaction Trans-resveratrol Tachiya model