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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Updated: Aug 12, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Food protein-derived amyloids do not accelerate amyloid β aggregation.

M Mahafuzur Rahman¹, Rodrigo Sanches Pires¹, Anja Herneke²

¹Department of Chemistry, KTH Royal Institute of Technology, Teknikringen 30, 100 44, Stockholm, Sweden.

Scientific Reports

|January 31, 2023

Summary

Food proteins forming amyloid structures do not accelerate amyloid-beta aggregation, a key factor in Alzheimer's disease. This research suggests dietary amyloid is unlikely to increase Alzheimer's risk.

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Last Updated: Aug 12, 2025

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

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Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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.