ArticleScientific reports2016
Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 77 citations in OpenAlex.
- The "Survivor Peptide" Hypothesis: Structural Resilience and Immunological Persistence of Food Allergens in the Gut-Mammary Axis.Nutrients · 2026Review
- Digestibility of Natural and Recombinant Allergenic Peanut Proteins in Artificial Gastrointestinal Fluids.Food safety (Tokyo, Japan) · 2025Article
- Investigation of Co-Assembly of Peanut Protein and Rice Protein: Effects on Protein Conformation and Immunoglobulin E Binding Capacity.Foods (Basel, Switzerland) · 2025Article
- Peanut allergen Ara h 6 is detectable in blood transfusion products.Clinical and translational allergy · 2023Article
- Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies.Antioxidants (Basel, Switzerland) · 2023Review
- The Effects of Peanut Oligopeptides on Exercise-Induced Fatigue in Mice and Its Underlying Mechanism.Nutrients · 2023Article
- INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity.Foods (Basel, Switzerland) · 2022Article
- Scientific Opinion on development needs for the allergenicity and protein safety assessment of food and feed products derived from biotechnology.EFSA journal. European Food Safety Authority · 2022Article
- The Effector Function of Allergens.Frontiers in allergy · 2022Review
- The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds.The Journal of allergy and clinical immunology · 2021Review
- Statement onEFSA journal. European Food Safety Authority · 2021Article
- Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation.Foods (Basel, Switzerland) · 2020Article
- Marine Bioactive Peptides-An Overview of Generation, Structure and Application with a Focus on Food Sources.Marine drugs · 2020Review
- Heat-Stable Hazelnut Profilin: Molecular Dynamics Simulations and Immunoinformatics Analysis.Polymers · 2020Article
- A multiple reaction monitoring method for determining peanut (Arachis hypogea) allergens in serum using quadrupole and time-of-flight mass spectrometry.Analytical and bioanalytical chemistry · 2020Article
- pH-Induced Local Unfolding of the Phl p 6 Pollen Allergen From cpH-MD.Frontiers in molecular biosciences · 2020Article
- Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1.Frontiers in molecular biosciences · 2020Article
- Article
- Stability of allergens.Molecular immunology · 2018Review
- Overexpression of biologically safe Rorippa indica defensin enhances aphid tolerance in Brassica juncea.Planta · 2017Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conglutins represent the major peanut allergens and are renowned for their resistance to gastro-intestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
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