Food protein-derived amyloids do not accelerate amyloid β aggregation

Area of Science:

• Biochemistry
• Neuroscience
• Food Science

Background:

• Protein misfolding into amyloid fibrils is linked to neurodegenerative diseases like Alzheimer's.
• Non-pathogenic proteins can form amyloid structures, raising concerns about cross-seeding with disease-associated amyloids.
• Food proteins can form amyloid under cooking conditions, posing potential dietary risks.

Purpose of the Study:

• To investigate the potential cross-seeding of amyloid-beta (Aβ) aggregation by amyloid fibrils derived from common food proteins.
• To determine if food-derived amyloid structures can accelerate or influence the formation of Aβ amyloid.

Main Methods:

• Kinetic studies using thioflavin T fluorescence assay.
• Investigated cross-seeding potential of 16 types of food protein-derived amyloid fibrils with amyloid-beta (Aβ).

Main Results:

• None of the 16 tested food protein-derived amyloid fibrils accelerated Aβ aggregation.
• Amyloid fibrils from hen egg lysozyme and oat protein isolate retarded Aβ aggregation.
• Observed retardation is attributed to interactions between food protein seeds and aggregated Aβ.

Conclusions:

• Food-derived amyloid structures do not appear to be a risk factor for initiating or accelerating Aβ pathology.
• Dietary amyloid is unlikely to contribute to the development of Alzheimer's disease.
• Further research into protein-protein interactions in amyloid formation is warranted.