ArticleFoods (Basel, Switzerland)2021
Characterization of Soybean Protein Isolate-Food Polyphenol Interaction via Virtual Screening and Experimental Studies.
Article in Foods (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 34 citations in OpenAlex.
- Enhanced Activity of Eugenol Pickering Emulsion Using Lactoferrin-Chlorogenic Acid Complex as a Green Stabilizer.Chemistry & biodiversity · 2026Article
- Dialdehyde Cellulose Nanocrystals and Proanthocyanidins Reinforced Soy Protein Isolate Films for Blueberry Preservation.Polymers · 2025Article
- Virtual Screening of Kelch-like ECH-Associated Protein 1-Nuclear Factor Erythroid 2-Related Factor 2 (Keap1-Nrf2) Inhibitors and In Vitro Validation.Molecules (Basel, Switzerland) · 2025Article
- Breaking barriers: Elevating legume protein functionality in food products through non-thermal technologies.Food chemistry: X · 2025Review
- Effect of Mono- and Polysaccharide on the Structure and Property of Soy Protein Isolate during Maillard Reaction.Foods (Basel, Switzerland) · 2024Article
- Virtual Screening of Soybean Protein Isolate-Binding Phytochemicals and Interaction Characterization.Foods (Basel, Switzerland) · 2023Article
- Changes on the conformational and functional properties of soybean protein isolate induced by quercetin.Frontiers in nutrition · 2022Article
- Structural changes and molecular mechanism study on the inhibitory activity of epigallocatechin against α-glucosidase and α-amylase.Frontiers in nutrition · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
(1) Background: Protein-polyphenol interactions have been widely studied regarding their influence on the properties of both protein and the ligands. As an important protein material in the food industry, soybean protein isolate (SPI) experiences interesting changes through polyphenols binding. (2) Methods: In this study, a molecular docking and virtual screening method was established to evaluate the SPI-polyphenol interaction. A compound library composed of 33 commonly found food source polyphenols was used in virtual screening. The binding capacity of top-ranking polyphenols (rutin, procyanidin, cyanidin chloride, quercetin) was validated and compared by fluorescence assays. (3) Results: Four out of five top-ranking polyphenols in virtual screening were flavonoids, while phenolic acids exhibit low binding capacity. Hydrogen bonding and hydrophobic interactions were found to be dominant interactions involved in soybean protein-polyphenol binding. Cyanidin chloride exhibited the highest apparent binding constant (Ka), which was followed by quercetin, procyanidin, and rutin. Unlike others, procyanidin addition perturbed a red shift of SPI fluorescence, indicating a slight conformational change of SPI. (4) Conclusions: These results suggest that the pattern of SPI-polyphenol interaction is highly dependent on the detailed structure of polyphenols, which have important implications in uncovering the binding mechanism of SPI-polyphenol interaction.
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