Study On The Interaction Of Proteins And Diethy1 Flavone-7-yi Phosphate And Diethy1 Flavone-5,7-y1 Phosphate By Fluorescence Method

Fluorescence method was used to study the interactions between lysozyme, myglobal, and bovine serum albumin and tow phosphorylated flavonoids and two flavonoids . The results showed that the phosphorylated flavonoids could form non-covalent complexes with lysozyme, myglobal, and bovine serum albumin while the flavonoids cannot. The results showed higher binding affinity between the proteins and the phosphorylated flavonoids than flavonoids did. The association constants of lysozyme, myglobal, and bovine serum albumin and the phosphorylated flavonoids were determined from a double reciprocal Lineweaver-Burk plot. The binding constants are foot:=1-68 104 L/mol and k3TC =1.06 104 L/mol (lysozyme-Diethyl Flavone-7-yl Phosphate), respectively. And so on. Experiments demonstrated that the higher the temperature were, the lower the slops of quenching curve of proteins were in presence of different amounts of the phosphorylated flavonoids. It was confirmed that the combinations for the phosphorylated flavonoids with the three proteins were single static quenching processes. According to the Foster dipole-dipole energy transfer, the distance to be measured between the phosphorylated flavonoids and tryptophane. From thermo dynamical coordination it could be judged that the binding power between the phosphorylated flavonoids and, myglobal, and bovine serum albumin were static electric power.Fluorescence in this paper provides good information about the phosphorylated flavonoids-proteins interactions. Moreover, the rapidity of data acquisition and the relative simplicity of interpretation make fluorescence a powerful tool for screening numerous small molecule-protein complexes.