Abstrait

Study On The Interaction Of Bovine Serum Albumin And Diethyl Flavone-7-yl phosphate By Fluorescence Method

Qu Lingbo, Chen Xiaolan, Zhao Yufen

Fluorescence method was used to study the interactions between BSA and diethyl flavone-7-yl phosphate and 7-hydroxyflavone. The results showed that the phosphorylated flavonoid can form non-covalent complexes BSA and showed higher binding affinity with the protein than 7- hydroxyflavone did. The association constants of BSA and diethyl flavone- 7-yl phosphate were determined from a Line weaver-Burk plot. Experiments demonstrated that the higher the temperature was, the lower the slops of quenching curve of BSA was in presence of different amounts of diethyl flavone-7-yl phosphate. It was confirmed that the combination for diethyl flavone-7-yl phosphate with BSA was a single static quenching process. According to the nonradiative transfer of energy, the distance was measured between the diethyl flavone-7-yl phosphate and tryptophane. From thermo dynamical coordination it could be judged that the binding power between diethyl flavone-7-yl phosphate and BSA was static electric power and. hydrophobic force.