The activities of amyloids from a structural perspective

• Published in: Nature (London) 2016-11, Vol.539 (7628), p.227-235
• Main Authors: Riek, Roland, Eisenberg, David S.
• Format: Article
• Language: English
• Subjects: 631/378; 631/535; 631/57; alpha-Synuclein - biosynthesis; alpha-Synuclein - chemistry; alpha-Synuclein - toxicity; Alzheimer's disease; Amyloid - biosynthesis; Amyloid - chemistry; Amyloid - metabolism; Amyloid - toxicity; Amyloid beta-Peptides - biosynthesis; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - toxicity; Animals; Development and progression; Disease; Glycoproteins; Health aspects; Humanities and Social Sciences; Humans; Hydrogen bonds; Models, Molecular; Molecular structure; multidisciplinary; Pathogenesis; Peptides; Prions - biosynthesis; Prions - chemistry; Prions - classification; Prions - toxicity; Protein Structure, Secondary; Proteins; review-article; Science
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/nature20416

The aggregation of proteins into structures known as amyloids is observed in many neurodegenerative diseases, including Alzheimer's disease. Amyloids are composed of pairs of tightly interacting, many stranded and repetitive intermolecular β-sheets, which form the cross-β-sheet structure. This structure enables amyloids to grow by recruitment of the same protein and its repetition can transform a weak biological activity into a potent one through cooperativity and avidity. Amyloids therefore have the potential to self-replicate and can adapt to the environment, yielding cell-to-cell transmissibility, prion infectivity and toxicity.