Chemical and Pharmaceutical Bulletin · 2003 · 101 citations · 10 references
Natural SciencesBiochemistryBiophysicsBiophysical ChemistryMolecular BiophysicsProtein BiochemistryBinding AffinityBinding KineticsBinding ThermodynamicsBiomolecular ThermodynamicsLigand BindingProtein BindingBovine Serum AlbuminEquilibrium Binding ConstantHydrophobic Interaction TheoryProtein-ligand Binding ThermodynamicsProtein-protein Binding ThermodynamicsQuenchingThermodynamic AnalysisVan 'T Hoff Equation
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.
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Atomic structure and chemistry of human serum albumin
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