Food protein-derived amyloids do not accelerate amyloid β aggregation

Abstract

The deposition of proteins in the form of amyloid fibrils is closely associated with several serious diseases. The events that trigger the conversion from soluble functional proteins into insoluble amyloid are not fully understood. Many proteins that are not associated with disease can form amyloid with similar structural characteristics as the disease-associated fibrils, which highlights the potential risk of cross-seeding of disease amyloid by amyloid-like structures encountered in our surrounding. Of particular interest are common food proteins that can be transformed into amyloid under conditions similar to cooking. We here investigate cross-seeding of amyloid-β (Aβ), a peptide known to form amyloid during the development of Alzheimer’s disease, by 16 types of amyloid fibrils derived from food proteins or peptides. Kinetic studies using thioflavin T fluorescence as output show that none of the investigated protein fibrils accelerates the aggregation of Aβ. In at least two cases (hen egg lysozyme and oat protein isolate) we observe retardation of the aggregation, which appears to originate from interactions between the food protein seeds and Aβ in aggregated form. The results support the view that food-derived amyloid is not a risk factor for development of Aβ pathology and Alzheimer’s disease.

From Fundamental Amyloid Protein Self-Assembly to Development of Bioplastics

“…In addition to substituting for traditional plastic materials, amyloid self-assemblies can also be used for broad biomedical engineering applications due to the benefits they provide such as nontoxicity, cell adhesion, and biocompatibility . Amyloids derived from food sources do not accelerate amyloid-β aggregation, which indicates that the application of food-based amyloid biomaterials is not likely to trigger diseases of protein misfolding . It has been shown that egg white protein lysosomes can self-assemble into microgels that could potentially be used as carriers for drug delivery purposes .…”

“… 172 Amyloids derived from food sources do not accelerate amyloid-β aggregation, which indicates that the application of food-based amyloid biomaterials is not likely to trigger diseases of protein misfolding. 173 It has been shown that egg white protein lysosomes can self-assemble into microgels that could potentially be used as carriers for drug delivery purposes. 41 With the help of microfluidics, lysosome molecules can self-assemble on the interface of water-in-oil or oil-in-water droplets.…”

Health concerns about possible long-term effects of legally marketed milk and dairy from animals with intramammary infections

“…Recently, a concern has been raised that AA amyloid in the human food chain could represent a possible biohazard ( 103 ). On that behalf, it was investigated whether amyloid seeds from different food proteins (lysozyme, β-lactoglobulin, soybean, mung bean, fava bean, lupine, potato, oat) affected the kinetics of Aβ 1−42 amyloid formation, which is the particular variant associated with Alzheimer's disease ( 104 ). None of the tested seeds had fibrillation-promoting effects.…”

Nordic Crops as Alternatives to Soy—An Overview of Nutritional, Sensory, and Functional Properties

“…This has led to a concern that PNFs made from food protein could have a seeding effect on the disease-related amyloids. However, a newly published study by Rhaman et al (2023) showed that PNFs from proteins such as faba bean and oat do not accelerate the aggregation of amyloid-β (Aβ), a peptide related to the development of Alzheimer’s disease [ 189 ]. This result indicates that plant-based PNFs have a future as texture enhancers in future food applications.…”