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

@article{Xiao2008ProbingTI,
  title={Probing the Interaction of Trans-resveratrol with Bovine Serum Albumin: A Fluorescence Quenching Study with Tachiya Model},
  author={Jian Xiao and Xiao Qing Chen and Xiangpin Jiang and Maciej Hilczer and Masanori Tachiya},
  journal={Journal of Fluorescence},
  year={2008},
  volume={18},
  pages={671-678}
}
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… CONTINUE READING
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