Interaction mechanism of flavonoids with whey protein isolate: A spectrofluorometric and theoretical investigation
| Autor: | Ruijie Shi, Jialun Hu, Guizhao Liang, Jiaqi Li, Zhanmei Jiang, Ran Tian |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Flavonoid
Substituent Quantitative Structure-Activity Relationship 01 natural sciences Analytical Chemistry Whey protein isolate chemistry.chemical_compound Residue (chemistry) 0404 agricultural biotechnology chemistry.chemical_classification Flavonoids biology Chemistry Hydrogen bond 010401 analytical chemistry Tryptophan food and beverages Hydrogen Bonding 04 agricultural and veterinary sciences General Medicine 040401 food science Fluorescence 0104 chemical sciences Molecular Docking Simulation Spectrometry Fluorescence Whey Proteins Biochemistry Polyphenol biology.protein Lactalbumin Thermodynamics Hydrophobic and Hydrophilic Interactions Food Science Protein Binding |
| Zdroj: | Food chemistry. 355 |
| ISSN: | 1873-7072 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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