Spectroscopic studies on the interaction of bovine serum albumin with ginkgolic acid: Binding characteristics and structural analysis

► GA binds to Sudlow's site II in BSA and form a 1:1 complex with it. ► GA quenches the fluorescence of BSA in a static profile. ► Main hydrophobic forces and binding distance between them are determined. ► GA binding results in an increased hydrophobicity around tryptophans in BSA. ► GA binding causes a decrease in α-helix and an increase in β-sheet substructures.