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Peer-reviewedCC BYBiotech (Basel (Switzerland))

Plant Proteins and Bioactive Peptides: Distinguishing Nutritional Quality from Sequence-Dependent Bioactivity.

  1. 1Scientific and Production Center "Armbiotechnology" RA, 14 Gyurjyan Str., Yerevan 0056, Armenia.
  2. 2Institute of Pharmacy, Yerevan State University, 1 Alex Manoogian Str., Yerevan 0025, Armenia.
  3. 3Institute of Biostructures and Bioimaging (IBB), Italian National Council for Research (CNR), Area di Ricerca Site and Headquarters, Via Pietro Castellino 111, 80131 Naples, Italy.

Abstract

Plant proteins represent both important nutritional resources and reservoirs of encrypted bioactive peptide sequences. However, protein nutritional quality and peptide bioactivity are distinct properties: a favorable indispensable amino acid profile or high digestibility does not necessarily predict the generation of biologically active peptides. This review examines plant-derived proteins and peptides with particular emphasis on the relationship between parent-protein composition, peptide release, sequence-dependent activity, analytical identification, and biological validation. The relevant peer-reviewed literature was critically evaluated, with detailed search and selection criteria. Major plant protein sources, peptide-generation strategies, purification and mass-spectrometric characterization approaches, and reported antioxidant, antimicrobial, antihypertensive, antidiabetic, anti-inflammatory, and other regulatory activities are discussed. Particular attention is given to experimentally validated peptide sequences and to the hierarchy of evidence from computational prediction and biochemical assays to cellular, animal, and human studies. Structure-activity relationships are interpreted cautiously, recognizing that peptide length, charge, hydrophobicity, and individual amino acid residues are contributory rather than independently predictive features. The review further integrates computational prediction with experimental validation and highlights gastrointestinal stability, intestinal transport, bioavailability, safety, scalability, and regulatory considerations as major translational challenges. This evidence-based framework distinguishes nutritional adequacy from peptide function and supports more rigorous development of plant-derived bioactive peptides for functional-food, nutraceutical, and related applications.

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BibTeX
@article{sargsyan2026plant,
  title = {{Plant Proteins and Bioactive Peptides: Distinguishing Nutritional Quality from Sequence-Dependent Bioactivity.}},
  author = {Tatevik Sargsyan and Heghine Hakobyan and Hasmik Grigoryan and Lala Stepanyan and Anahit Hovhannisyan and Zhaklina Saribekyan and Avetis Tsaturyan and Nelli Hovhannisyan and Ashot Saghyan and Caterina Vicidomini and Rosanna Palumbo and Giovanni N Roviello},
  journal = {Biotech (Basel (Switzerland))},
  year = {2026},
  month = oct,
  doi = {10.3390/biotech15040089},
  url = {https://europepmc.org/article/MED/42930066},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - Plant Proteins and Bioactive Peptides: Distinguishing Nutritional Quality from Sequence-Dependent Bioactivity.
AU  - Tatevik Sargsyan
AU  - Heghine Hakobyan
AU  - Hasmik Grigoryan
AU  - Lala Stepanyan
AU  - Anahit Hovhannisyan
AU  - Zhaklina Saribekyan
AU  - Avetis Tsaturyan
AU  - Nelli Hovhannisyan
AU  - Ashot Saghyan
AU  - Caterina Vicidomini
AU  - Rosanna Palumbo
AU  - Giovanni N Roviello
PY  - 2026
DA  - 2026/10/07
JO  - Biotech (Basel (Switzerland))
DO  - 10.3390/biotech15040089
UR  - https://europepmc.org/article/MED/42930066
AB  - Plant proteins represent both important nutritional resources and reservoirs of encrypted bioactive peptide sequences. However, protein nutritional quality and peptide bioactivity are distinct properties: a favorable indispensable amino acid profile or high digestibility does not necessarily predict the generation of biologically active peptides. This review examines plant-derived proteins and peptides with particular emphasis on the relationship between parent-protein composition, peptide release, sequence-dependent activity, analytical identification, and biological validation. The relevant peer-reviewed literature was critically evaluated, with detailed search and selection criteria. Major plant protein sources, peptide-generation strategies, purification and mass-spectrometric characterization approaches, and reported antioxidant, antimicrobial, antihypertensive, antidiabetic, anti-inflammatory, and other regulatory activities are discussed. Particular attention is given to experimentally validated peptide sequences and to the hierarchy of evidence from computational prediction and biochemical assays to cellular, animal, and human studies. Structure-activity relationships are interpreted cautiously, recognizing that peptide length, charge, hydrophobicity, and individual amino acid residues are contributory rather than independently predictive features. The review further integrates computational prediction with experimental validation and highlights gastrointestinal stability, intestinal transport, bioavailability, safety, scalability, and regulatory considerations as major translational challenges. This evidence-based framework distinguishes nutritional adequacy from peptide function and supports more rigorous development of plant-derived bioactive peptides for functional-food, nutraceutical, and related applications.
SN  - 2673-6284
ER  -