Fluorescence studies on the interactions of barbaloin with bovine serum albumin.
The fluorescence quenching reactions of barbaloin with bovine serum albumin (BSA) in pH 7.20 Tris-HCl buffer solution were studied. The quenching mechanism of BSA by barbaloin was interpreted using the Stern-Volmer (S-V) mechanism. The binding constant K values were 2.78 x 10(5) (293 K), 1.87 x 10(5) (310 K), 1.25 x 10(5) (318 K), and the number of binding sites (n) were 1.18, 1.14, and 1.09, respectively. In addition, the thermodynamic functions enthalpy (deltaH degrees ) and entropy (deltaS degrees ) for the reaction were also calculated according to Vant's Hoff equation were -23.7 kJ/mol and 23.6 J/mol, respectively. Plausible explanations of the quenching mechanism are discussed on the basis of a hydrophobic interaction between barbaloin and BSA.
Tian
Jianniao
J
Department of Chemistry, Lanzhou University, China.
Liu
Jiaqin
J
Zhang
Jiyou
J
Hu
Zhide
Z
Chen
Xinguo
X
D000465:Algorithms; D000818:Animals; D000873:Anthracenes / Q000737:chemistry / Q000378:metabolism*; D002400:Cathartics / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D007700:Kinetics; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
D000873:Anthracenes; D002400:Cathartics; C045601:barbaloin; D012710:Serum Albumin, Bovine