Fluorescence Studies on the Interactions of Barbaloin with Bovine Serum Albumin

• DOI: 10.1248/cpb.51.579
• Publication Date: 2003-05-01T06:03:04Z
• Authors: Jianniao Tian; Jiaqin Liu; Jiyou Zhang; Zhide Hu; Xinguo Chen
• Keywords: Bovine serum albumin; Hydrophobic effect; Binding constant

The fluorescence quenching reactions of barbaloin with bovine serum albumin (BSA) in pH 7.20 Tris-HCl buffer solution were studied. mechanism BSA by was interpreted using the Stern-Volmer (S-V) mechanism. binding constant K values 2.78 x 10(5) (293 K), 1.87 (310 1.25 (318 and number sites (n) 1.18, 1.14, 1.09, respectively. In addition, thermodynamic functions enthalpy (deltaH degrees ) entropy (deltaS for reaction also calculated according to Vant's Hoff equation -23.7 kJ/mol 23.6 J/mol, Plausible explanations are discussed on basis a hydrophobic interaction between BSA.