The interaction mechanism between whey protein isolate (WPI) and flavonoids was investigated based on the spectrofluorometric and theoretical methods in this study. The binding capacities of 15 flavonoids with WPI were compared. Then, the 3D-QSAR model describing their binding behavior was established to illustrate the effect of flavonoid structure on binding. It was found that the flavonoids with electronegative group at C-3 or large substituent at C-3 and C-7 possessed high binding performance. The thermodynamic analysis further indicated the hydrophobic force was the main driving force for binding of WPI and flavonoids. Both synchronous and 3D fluorescence analysis suggested that the microenvironment around tryptophan residues had changed, which coincided with the result of molecular docking that tryptophan residue of α-lactalbumin contributed significantly to hydrogen bonding. Our results suggested that the combination of 3D-QSAR and molecular docking may prompt the interaction research between food-derived proteins and polyphenols.
Keywords: 3D-QSAR; Flavonoids; Interaction; Molecular docking; Whey protein isolate.
Copyright © 2021 Elsevier Ltd. All rights reserved.