Affordable Access

deepdyve-link deepdyve-link
Publisher Website

Probing the interaction of trans-resveratrol with bovine serum albumin: a fluorescence quenching study with Tachiya model.

Authors
  • Xiao, J B1
  • Chen, X Q
  • Jiang, X Y
  • Hilczer, M
  • Tachiya, M
  • 1 College of Chemistry and Chemical Engineering, Central South University, Changsha, People's Republic of China. , (China)
Type
Published Article
Journal
Journal of fluorescence
Publication Date
Jan 01, 2008
Volume
18
Issue
3-4
Pages
671–678
Identifiers
DOI: 10.1007/s10895-008-0346-x
PMID: 18351302
Source
Medline
License
Unknown

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 x 10(4) (293.15 K), 8.89 x 10(4) (303.15 K) and 1.60 x 10(5) 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.

Report this publication

Statistics

Seen <100 times