Delineating the interaction mechanism of glabridin and ovalbumin by spectroscopic and molecular docking techniques.

The interaction between ovalbumin (OVA) and isoflavonoid glabridin (GB) was investigated using spectroscopic and molecular docking techniques. Fluorescence spectroscopy revealed that GB was bound to OVA mainly due to hydrogen bonding and hydrophobic forces. FT-IR spectroscopy showed that the combination of GB and OVA resulted in a decrease in the β-sheet content of OVA and an increase in the α-helix and extended-chain content. All these experimental results were supported and clarified by molecular docking simulations. GB binding was able to inhibit chemical denaturant-induced structural changes in OVA as observed by intrinsic tryptophan and ANS fluorescence. Moreover, GB-OVA complex increased the aqueous solubility of GB by about 4.45 times at pH 7.0. These results provided insights into the interaction between GB and OVA that contributes to the utilization of GB in the food and pharmaceutical industries.