A steady‐state and time‐resolved fluorescence, circular dichroism study on the binding of myricetin to bovine serum albumin

• DOI: 10.1002/bio.1124
• Publication Date: 2009-05-29T04:05:42Z
• Authors: Jianniao Tian; Yanchun Zhao; Xiuhong Liu; Shulin Zhao
• Keywords: Bovine serum albumin

Abstract The binding mechanism of myricetin (Myr) to bovine serum albumin was investigated by using steady‐state and time‐resolved fluorescence circular dichroism. results the quenching experiment indicate that it is a static process ( C Myr / BSA ≤ 3) at low quencher concentration site located near Trp212 residue. association constants different temperatures were calculated. From thermodynamic parameters, enthalpy change (Δ H 0 ), Gibbs free energy G ) entropy S obtained in experiment, found hydrophobic electrostatic interactions play important roles BSA. According Föster transfer theory, separation distance, r , efficiency, E radius, R from above experiments can be tightly bound Then, effects ionic strength, metal ion, pH surfactants on investigated, which also showed major role process. On other hand, conformation secondary structure further studied through dichroism synchronous spectra. It had changed after interaction with Myr. study short lifetime decreased addition Myr, implies buried Trp 212 main site. Copyright © 2009 John Wiley & Sons, Ltd.