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

Abstract

The interaction between ginkgolic acid (GA, C15:0) and bovine serum albumin (BSA) is investigated by several spectroscopic methodologies. At first, the binding characteristics of GA and BSA are determined by fluorescence emission spectra. It is showed that GA quenches the fluorescence of BSA and the static quenching constant KLB is 11.7891×104Lmol−1s−1 at 297K. GA and BSA form a 1:1 complex with a binding constant of 9.12×105Lmol−1. GA binds to the Sudlow's drug binding site II in BSA, and the binding distance between them is calculated as 1.63nm based on the Förster theory. The thermodynamic parameters indicate that the interaction between BSA and GA is driven mainly by hydrophobic forces. On the other hand, structural analysis indicates that GA binding results in an increased hydrophobicity around the tryptophan residues of BSA as revealed by the synchronous fluorescence spectra, and a decrease in α-helix as revealed by the far-UV CD spectra. In addition, ANS, UV–vis and RLS experiments confirmed that GA binding causes a certain structural changes in BSA. These findings provide the binding information between BSA and GA, and may be helpful for pharmacokinetics and the design of dosage forms of GA.