Protein–polyphenol interactions enhance the antioxidant capacity of phenolics: analysis of rice glutelin–procyanidin dimer interactions

Dai, Taotao; Chen, Jun; McClements, David Julian; Hu, Peng; Ye, Xiaoqin; Liu, Chengmei; Li, Ti

doi:10.1039/c8fo02246a

Cited by 252Proteins in Food SystemsProtein Interaction Studies and Fluorescence AnalysisProtein Hydrolysis and Bioactive Peptides

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Protein–polyphenol interactions enhance the antioxidant capacity of phenolics: analysis of rice glutelin–procyanidin dimer interactions

Dai, Taotao, Chen, Jun, McClements, David Julian, Hu, Peng, Ye, Xiaoqin, Liu, Chengmei, Li, Ti·2019·Food & Function

DOI 10.1039/c8fo02246a

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Abstract

Rice glutelin and procyanidins are often used in functional foods as sources of plant-based proteins and polyphenols, respectively, but little is currently known about the interactions between them.

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Hydroxyl groups of polyphenols could insert into hydrophobic regions of protein molecules, disrupting the hydrogen bonding network that stabilized α-helixes.
“Specifically, the hydroxyl groups of polyphenols could insert into the hydrophobic regions of protein molecules, disrupting the hydrogen bonding network that stabilized α‐helixes (T. Dai et al. 2019).”
From Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion (2026) · cites this paper as T. Dai et al. 2019

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Authors: Dai, T., Chen, J., McClements, D. J., Hu, P., Ye, X., Liu, C., & Li, T.
Affiliations: Nanchang University (CN)
Amherst College (US)
Corresponding author: McClements, David Julian
Li, Ti
ORCID: Dai, Taotao
Chen, Jun
McClements, David Julian
Ye, Xiaoqin
Liu, Chengmei
Li, Ti
Venue: Food & Function
Publisher: Royal Society of Chemistry (RSC)
Published: 2019
Volume: 10
Issue: 2
Pages: 765-774
ISSN: 2042-6496 (ISSN-L)
2042-650X
DOI: 10.1039/c8fo02246a
OpenAlex: W2912138721
Cited by: 252
References: 0
Citations by year: 2026: 22 · 2025: 34 · 2024: 41 · 2023: 48 · 2022: 38 · 2021: 41 · 2020: 23 · 2019: 5
FWCI: 20.64
Type: journal article
Language: en
Open access: closed
Licence: rsc.li/journals-terms-of-use#chorus (am, 386 d)
Locations: Food & Function (publishedVersion)
PubMed (publishedVersion)
Funders: National Natural Science Foundation of China (31460394, 31760441)
National Institute of Food and Agriculture (MAS00491)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
Keywords: rice glutelin, procyanidin B2, protein-polyphenol interactions, antioxidant capacity, protein secondary structure, protein hydrophobicity, emulsion stability, hydrophobic interactions, molecular docking, functional foods, plant proteins, polyphenols
MeSH terms: Antioxidants, Catechin, Computer Simulation, Glutens, Models, Chemical, Models, Molecular, Protein Conformation, Oryza, Spectrophotometry, Ultraviolet, Proanthocyanidins, Biflavonoids, Polyphenols

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Protein–polyphenol interactions enhance the antioxidant capacity of phenolics: analysis of rice glutelin–procyanidin dimer interactions

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