Context (archaeology)

Amyloid fibril

Food protein

Biology

Materials science

Amyloid (mycology)

Biochemistry

Inorganic chemistry

Fibril

Environmental health

Paleontology

Nanotechnology

Bioinformatics

Biomedicine

Characterization (materials science)

Amyloid β

Medicine

Chemistry

Biophysics

Protein aggregation

Disease

Human health

Pathology

Advances in Colloid and Interface Science

Amyloid fibrils have traditionally been considered only as pathological aggregates in human neurodegenerative diseases, but it is increasingly becoming clear that the propensity to form amyloid fibrils is a generic property for all proteins, including food proteins. Differently from the pathological amyloid fibrils, those derived from food proteins can be used as advanced materials in biomedicine, tissue engineering, environmental science, nanotechnology, material science as well as in food science, owing to a combination of highly desirable feature such as extreme aspect ratios, outstanding stiffness and a broad availability of functional groups on their surfaces. In food science, protein fibrillization is progressively recognized as an appealing strategy to broaden and improve food protein functionality. This review article discusses the various classes of reported food protein amyloid fibrils and their formation conditions. It furthermore considers amyloid fibrils in a broad context, from their structural characterization to their forming mechanisms and ensued physical properties, emphasizing their applications in food-related fields. Finally, the biological fate and the potential toxicity mechanisms of food amyloid fibrils are discussed, and an experimental protocol for their health safety validation is proposed in the concluding part of the review.

Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications