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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Recent Insights into Protein-Polyphenol Complexes: Molecular Mechanisms, Processing Technologies, Synergistic

Hoang Duy Huynh1,2,3, Thanh Huong Tran Thi3, Thanh Xuan Tran Thi3

  • 1Department of Seafood Science, National Kaohsiung University of Science and Technology, Kaohsiung 81157, Taiwan.

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Grafting proteins with polyphenols creates beneficial complexes. These protein-polyphenol complexes enhance food ingredients, improve polyphenol stability and bioavailability, and offer sustainable applications.

Keywords:
bioactive compoundsmolecular mechanismspreservationprotein-polyphenol complexessynergistic effects

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Area of Science:

  • Food Science
  • Biochemistry
  • Materials Science

Background:

  • Protein modification via polyphenol grafting is gaining attention.
  • Protein-polyphenol interactions (covalent and non-covalent) offer green strategies for food ingredient development.
  • These complexes enhance polyphenol stability, biological activity, and bioavailability.

Purpose of the Study:

  • To review binding affinities and interaction mechanisms of protein-polyphenol complexes.
  • To explore factors influencing complex formation and protein structural modulation.
  • To discuss processing technologies and synergistic bioactivities for novel applications.

Main Methods:

  • Literature review focusing on protein-polyphenol interactions.
  • Analysis of factors affecting complex formation and structural changes.
  • Systematic discussion of synergistic bioactivities and applications.

Main Results:

  • Protein-polyphenol complex formation alters structural and functional properties.
  • Complexes improve polyphenol bioavailability and stability.
  • Synergistic bioactivities are observed, with potential for enhanced nutritional and health benefits.

Conclusions:

  • Understanding protein-polyphenol interactions is key for developing novel functional ingredients and products.
  • These complexes offer sustainable solutions for food, pharmaceutical, and material engineering applications.
  • Applications include functional foods with extended shelf life and improved health aspects.