Abstrait

Fluorimetric Study of the Interaction of Daidzein with BSA

Song J, Yang L and Wang QM

The mutual interaction of daidzein with bovine serum albumin (BSA) was investigated by means of fluorescence spectroscopy. The results revealed that daidzein caused the fluorescence quenching of BSA through a static quenching procedure. The value of binding constant (Ka) were 1.17 × 104 M−1 (T=310K), 3.74 × 104 M−1 (T=303K), 5.36 × 104 M−1 (T=298K) respectively. Thermodynamic parameters ΔG0, ΔH0, ΔS0 were calculated, besides the van der Waals force and hydrogen bonds play a significant role in spontaneous stabilizing the complex. Moreover, the effect of Cu2+, Ni2+, Mn2+ and Co2+ on the binding constants between daidzein and BSA were studied.