Fuente: PubMed "plant biotechnology" Curr Protein Pept Sci. 2026 May 22. doi: 10.2174/0113892037462419260514104451. Online ahead of print.ABSTRACTFood Protein-derived Amyloid Fibrils (FPAFs) are rapidly gaining attention for their unique functional properties, offering new ways to improve texture and stability in plant-based and clean-label foods. These nanofibrils show superior gelling, emulsifying, and water-binding properties, supporting sustainable food innovation. However, the safety of FPAFs remains a topic of debate. In vitro gastrointestinal models show that fibrils from β-lactoglobulin and lysozyme are degraded into non-amyloidogenic oligopeptides during digestion, with no residual β-sheet-rich fragments left to induce further amyloid formation. In contrast, certain amyloid fibrils derived from legumes resist digestive enzymes and exhibit cytotoxicity in human epithelial cells at high concentrations. The presence of heat-stable amyloid A (AA) fibrils in animal-based products, such as foie gras, raises theoretical concerns about transmissible amyloidosis, especially in individuals with chronic inflammation. Most food-grade fibrils lack the pathogenic structures seen in disease-related amyloids, yet their potential to trigger protein misfolding or bypass intestinal barriers is under ongoing investigation. This review critically evaluates the dual nature of food protein-derived amyloid fibrils by integrating their functional advantages with emerging safety concerns. Future research must explore real food matrix effects, long-term exposure, and relevant biomarkers to clarify the safety of FPAFs. With strict regulation and comprehensive risk evaluation, FPAFs could sustainably transform food textures while minimizing potential health concerns.PMID:42227484 | DOI:10.2174/0113892037462419260514104451