The activities of amyloids from a structural perspective.
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.
Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zurich, 8093 Zürich, Switzerland.
Roland
R
Riek
UCLA-DOE Institute, Los Angeles, California 90095-1570, USA.|Howard Hughes Medical Institute, Los Angeles, California 90095-1570, USA.
David S
DS
Eisenberg
D000682:Amyloid / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism* / Q000633:toxicity; D016229:Amyloid beta-Peptides / Q000096:biosynthesis / Q000737:chemistry / Q000633:toxicity; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D011328:Prions / Q000096:biosynthesis / Q000737:chemistry / Q000145:classification / Q000633:toxicity; D017433:Protein Structure, Secondary; D051844:alpha-Synuclein / Q000096:biosynthesis / Q000737:chemistry / Q000633:toxicity
D000682:Amyloid; D016229:Amyloid beta-Peptides; D011328:Prions; D051844:alpha-Synuclein