Ginkgolic acid C15:0

Journal of Luminescence Volume 132, Issue 5, May 2012, Pages 1207–1214

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

The interaction between Ginkgolic acid C15:0 and bovine serum albumin (BSA) is investigated by several spectroscopic methodologies.
METHODS AND RESULTS:
At first, the binding characteristics of Ginkgolic acid C15:0 and BSA are determined by fluorescence emission spectra. It is showed that Ginkgolic acid C15:0 quenches the fluorescence of BSA and the static quenching constant KLB is 11.7891×104 L mol−1 s−1 at 297 K. Ginkgolic acid C15:0 and BSA form a 1:1 complex with a binding constant of 9.12×105 L mol−1. Ginkgolic acid C15:0 binds to the Sudlow's drug binding site II in BSA, and the binding distance between them is calculated as 1.63 nm based on the Förster theory. The thermodynamic parameters indicate that the interaction between BSA and Ginkgolic acid C15:0 is driven mainly by hydrophobic forces. On the other hand, structural analysis indicates that Ginkgolic acid C15:0 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 Ginkgolic acid C15:0 binding causes a certain structural changes in BSA.
CONCLUSIONS:
These findings provide the binding information between BSA and Ginkgolic acid C15:0), and may be helpful for pharmacokinetics and the design of dosage forms of Ginkgolic acid C15:0.