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Updated: May 25, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity
1Max-Planck Research Unit for Enzymology of Protein Folding and Martin Luther University Halle-Wittenberg, Weinbergweg 22, 01620 Halle (Saale), Germany. fandrich@enzyme-halle.mpg.de
Abstract:
Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as Alzheimer's disease, Parkinson's disease and Huntington's disease. Focusing primarily on the oligomeric states formed from Alzheimer's disease β-amyloid (Aβ) peptide, this review will make references to other polypeptide systems, highlighting common principles or sequence-specific differences. The covered topics include the structural properties and polymorphism of oligomers, the biophysical mechanism of peptide self-assembly and its role for pathogenicity in amyloid disease. Oligomer-dependent toxicity mechanisms will be explained along with recently emerging possibilities of interference.
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