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  • Title: Comparing the binding interaction between β-lactoglobulin and flavonoids with different structure by multi-spectroscopy analysis and molecular docking.
    Author: Li T, Hu P, Dai T, Li P, Ye X, Chen J, Liu C.
    Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2018 Aug 05; 201():197-206. PubMed ID: 29753236.
    Abstract:
    Four kinds of flavonoids (apigenin, naringenin, kaempferol, genistein) were skillfully selected to investigate the interaction between flavonoids and β-lactoglobulin (β-LG) by multi-spectroscopy analysis and molecular docking. Hydrogenation on C2C3 double bond weakened the affinity of apigenin for β-LG and it's most obvious, followed by hydroxylation of C3 and position isomerism of phenyl ring B. The main interaction force for apigenin and naringenin binding to β-LG (van der Waals forces and hydrogen bonds) was different from that of genistein and kaempferol (hydrophobic interactions). Circular dichroism and fluorescence experiments indicated that conformation of β-LG became loose and surface hydrophobicity of β-LG was reduced in the presence of flavonoids. Molecular docking indicated that flavonoids interacted with specific amino acid residues located on the outer surface of β-LG. These findings can provide a deep understanding about the interaction mechanism between flavonoids and protein, and it may be valuable in dairy incorporation with flavonoids.
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