Protein-Polyphenol Interaction Dynamics and Characterization
Summary
Protein–polyphenol interactions underpin a diverse array of biological phenomena, from nutrient bioavailability to the stability and functionality of food and pharmaceutical formulations. These interactions occur through covalent bonds—often formed via enzymatic oxidation—and a spectrum of non-covalent forces including hydrogen bonding, hydrophobic interactions, van der Waals forces and π–π stacking. Binding events induce conformational alterations in the protein’s secondary and tertiary structure, which can be characterised by spectroscopic techniques such as fluorescence quenching, circular dichroism and Fourier transform infrared spectroscopy. Complementary computational approaches, notably molecular docking and dynamics simulations, have refined our understanding of binding sites, energetics and kinetic pathways. Environmental parameters—pH, temperature, ionic strength, pressure and ultrasound—profoundly influence the affinity, stoichiometry and stability of protein–polyphenol complexes. Thermodynamic parameters (ΔG, ΔH, ΔS) derived from isothermal titration calorimetry provide quantitative insights into driving forces, while particle-level analysis using dynamic light scattering and ζ-potential measurements informs on colloidal stability. This multifaceted characterisation framework has enabled the rational design of protein-based delivery systems, improved antioxidant efficacy and advanced the development of functional foods and nutraceutical carriers with enhanced digestibility, shelf life and targeted release properties.
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Protein-Polyphenol Interaction Dynamics and Characterization publication trend
The graph below shows the total number of articles in protein-polyphenol interaction dynamics and characterization across all publications each year (not limited to Nature Index journals).
Technical terms
Polyphenol: A class of plant-derived secondary metabolites with multiple phenolic rings.
Fluorescence quenching: The reduction in fluorescence emission upon interaction between a fluorophore and a quencher.
Molecular docking: A computational method to predict the preferred orientation and binding affinity of two interacting molecules.
Circular dichroism (CD): A spectroscopic technique that measures differential absorption of left and right circularly polarised light to assess protein secondary structure.
ζ-Potential: The electrical potential at the slipping plane of a particle in suspension, indicative of colloidal stability.
Bioavailability: The fraction of an ingested compound that reaches systemic circulation and is available at the site of action.
References
- Recent advances in the effect of ultrasound on the binding of protein−polyphenol complexes in foodstuff. Food Frontiers (2023).
- Co-assembled whey protein and proanthocyanidins as a promising biocarrier for hydrophobic pterostilbene: Fabrication, characterization, and cellular antioxidant potential. Journal of Dairy Science (2023).
- Study on the Interaction Mechanism of Theaflavin with Whey Protein: Multi-Spectroscopy Analysis and Molecular Docking. Foods (2023).
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