LAUSR

Mangiferin (MAG) is a kind of polyphenol with many bioactivities. However, its application in medicines and functional foods is restricted because of its poor aqueous solubility and stability. The construction of a MAG/protein complex is an effective way to solve this bottleneck. In this study, the interaction of MAG and ovalbumin (OVA) was systematically investigated by spectrofluorimetry, and their binding mode was clarified based on molecular docking. The results suggested that MAG could cause the static fluorescence quenching of OVA with the quenching constant (Kq) of >2 × 1010 L/(mol·s). Their binding performance increased with increasing temperature, and the binding-site number (n) was close to 1. The thermodynamic analysis indicated that the binding was a spontaneous process, which was mainly driven by hydrophobic force. During this process, there was no apparent change in the microenvironment surrounding the tyrosine and tryptophan residues of OVA. The molecular docking results demonstrated the hydrophobic interaction and hydrogen bonding in the complex, which well-confirmed the results of the fluorescence experiments.