ArticleNature communications2023
Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 116 citations in OpenAlex.
- Oat protein nanofibril-iron hybrids offer a stable, high-absorption iron delivery platform for iron fortification.Nature food · 2025Trial
- Protein Nanofibrils as Emerging Biomaterials for Sustainable Food Packaging: Advances, Challenges, and Future Opportunities.Comprehensive reviews in food science and food safety · 2026Review
- Engineered protein nanofibrils for chain-integrated water treatment: From source monitoring to end-point purification.Eco-Environment & Health · 2026Review
- Understanding the Effect of Zein-Resveratrol Interactions on the Mechanical and Functional Properties of Zein Gels.Gels (Basel, Switzerland) · 2026Article
- Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins.Nature communications · 2026Article
- Adhesion Mechanisms of Amyloid-Like Oligomer Monolayers Enabling Stable Surface Modification for Inert Polymers.JACS Au · 2026Article
- Protection and Delivery of Phytochemicals from Passive Encapsulation to Guaranteed Self-Assembly Induced by Amyloid Template for Chronic Disease Prevention via Modulating Microbial-Host Crosstalk.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Physicochemical properties of amyloid-like fibrils from ultrasonication-induced plum seed protein-catechin conjugates.Food chemistry: X · 2026Article
- Food-derived β-lactoglobulin nanofibrils: An efficacy, safe, and scalable solution to overcome oral insulin delivery challenges.Bioactive materials · 2026Article
- Piperlonguminine inhibits hen egg white lysozyme amyloid fibril formation and mitigates amyloid fibril-induced hepatocellular damage.Current research in food science · 2026Article
- The Reconstruction of Sesame Protein-Derived Amyloid Fibrils Alleviates the Gastric Digestion Instability of β-Carotene Nanoparticles.Nanomaterials (Basel, Switzerland) · 2025Article
- Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Ultrasound-Assisted Fibril Formation Enhances Complexation of Oat Globulin with Quercetin: Mechanism, Structure Evolution, Delivery Performance.Foods (Basel, Switzerland) · 2025Article
- Structural Insights and Functional Dynamics of β-Lactoglobulin Fibrils.Nano letters · 2025Article
- Impurities in amyloid studies: The power of automated model building within a cautionary tale for structural biologists.Protein science : a publication of the Protein Society · 2025Article
- Amyloid Fibrils of Pea Protein Isolated Induced by Cold Plasma Treatment and Its Stabilization on High Internal Phase Emulsions.Food science & nutrition · 2025Article
- Formation and Structural Characteristics of Heating-Induced Amyloid Fibrils Derived from Rice Albumin at Different pH Values.Foods (Basel, Switzerland) · 2025Article
- Nanostructure-Engineered Optical and Electrochemical Biosensing Toward Food Safety Assurance.Foods (Basel, Switzerland) · 2025Review
- Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions.Food chemistry: X · 2025Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption. By combining SDS-PAGE, ELISA, fluorescence, AFM, MALDI-MS, CD, microfluidics, and SAXS techniques for the characterization of β-lactoglobulin and lysozyme amyloid fibrils subjected to in-vitro gastrointestinal digestion, here we show that either no noticeable conformational differences exist between amyloid aggregates and their monomer counterparts after the gastrointestinal digestion process (as in β-lactoglobulin), or that amyloid fibrils are digested significantly better than monomers (as in lysozyme). Moreover, in-vitro exposure of human cell lines and in-vivo studies with C. elegans and mouse models, indicate that the digested fibrils present no observable cytotoxicity, physiological abnormalities in health-span, nor accumulation of fibril-induced plaques in brain nor other organs. These extensive in-vitro and in-vivo studies together suggest that the digested food amyloids are at least equally as safe as those obtained from the digestion of corresponding native monomers, pointing to food amyloid fibrils as potential ingredients for human nutrition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.