Interaction of amphiphilic pyrene derivatives with bovine serum albumin
In order to obtain the binding properties of water-soluble pyrene derivatives with serum albumin,the interaction between a pyrene derivative(C12PDA)and bovine serum albumin(BSA)in neutral buffer solution was studied.Firstly,the interaction between C12PDA and BSA was studied by absorption and fluorescence spectra.The results show that the fluorescence of BSA is quenched by C12PDA due to static quenching,and the hydrophobic effect is the dominant force in the complex forming.The effect of C12PDA on the conformation of BSA and its binding mode were studied by synchronous fluorescence,three-dimensional fluorescence,circular dichroism and molecular docking simulation.The results showed that there were intermolecular hydrogen bond interactions between C12PDA and several amino acid residues of BSA.Moreover,the content of α-helical structure of BSA was reduced by C12PDA.
NETL
NSTL
万方数据
