Interaction Between Serum Albumin and Four Flavones by Fluorescence Spectroscopy and Molecular Docking

Combined with molecular docking model using FlexX software, a fluorescence spectroscopy was used to investigate the interaction between bovine serum albumin (BSA) and four flavones, baicalein, baicalin, wogonin, and scutellarin, and their acting mechanism. Thus, the binding constant KA and the number of binding site n were determined. The results revealed that the binding site value between flavones and BSA was nearly 1, and the binding site was temperature independent. Baicalein and wogonin tended to bind with BSA mainly by hydrophobic interaction, whereas baicalin and scutellarin reacted with BSA mainly by hydrogen bond and van der Waals forces. Both fluorescence spectroscopy and molecular docking model are complimentary to each other for the investigation of the interaction between albumin and natural products from an experimental and theoretical view.