ArticleScientific reports2016
Commercial processed soy-based food product contains glycated and glycoxidated lunasin proteoforms.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Molecular Imprints of Clinical Comorbidities in Hypothalamic Extracellular Vesicles at the Onset of Obesity.ACS omega · 2025Article
- Proteomic Characterization of a Lunasin-Enriched Soybean Extract Potentially Useful in the Treatment ofNutrients · 2024Article
- Recent advances in exploring and exploiting soybean functional peptides-a review.Frontiers in nutrition · 2023Review
- Lunasin as a Promising Plant-Derived Peptide for Cancer Therapy.International journal of molecular sciences · 2022Review
- System-wide molecular dynamics of endothelial dysfunction in Gram-negative sepsis.BMC biology · 2020Article
- Brain-derived and circulating vesicle profiles indicate neurovascular unit dysfunction in early Alzheimer's disease.Brain pathology (Zurich, Switzerland) · 2019Article
- Maillard Proteomics: Opening New Pages.International journal of molecular sciences · 2017Review
- The synergy between natural polyphenol-inspired catechol moieties and plant protein-derived bio-adhesive enhances the wet bonding strength.Scientific reports · 2017Article
- LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics.Journal of visualized experiments : JoVE · 2017Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nutraceuticals have been proposed to exert positive effects on human health and confer protection against many chronic diseases. A major bioactive component of soy-based foods is lunasin peptide, which has potential to exert a major impact on the health of human consumers worldwide, but the biochemical features of dietary lunasin still remain poorly characterized. In this study, lunasin was purified from a soy-based food product via strong anion exchange solid phase extraction and then subjected to top-down mass spectrometry analysis that revealed in detail the molecular diversity of lunasin in processed soybean foods. We detected multiple glycated proteoforms together with potentially toxic advanced glycation end products (AGEs) derived from lunasin. In both cases, modification sites were Lys24 and Lys29 located at the helical region that shows structural homology with a conserved region of chromatin-binding proteins. The identified post-translational modifications may have an important repercussion on lunasin epigenetic regulatory capacity. Taking together, our results demonstrate the importance of proper chemical characterization of commercial processed food products to assess their impact on consumer's health and risk of chronic diseases.
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Registered trials
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