Structural studies of amyloid-β peptides: Unlocking the mechanism of aggregation and the associated toxicity

Rihards Aleksis*, Filips Oleskovs, Kristaps Jaudzems, Jens Pahnke, Henrik Biverstål

*Corresponding author for this work
30 Citations (Scopus)

Abstract

Alzheimer's disease (AD) is one of the most prevalent neurodegenerative diseases worldwide. Formation of amyloid plaques consisting of amyloid-β peptides (Aβ) is one of the hallmarks of AD. Several lines of evidence have shown a correlation between the Aβ aggregation and the disease development. Extensive research has been conducted with the aim to reveal the structures of the neurotoxic Aβ aggregates. However, the exact structure of pathological aggregates and mechanism of the disease still remains elusive due to complexity of the occurring processes and instability of various disease-relevant Aβ species. In this article we review up-to-date structural knowledge about amyloid-β peptides, focusing on data acquired using solution and solid state NMR techniques. Furthermore, we discuss implications from these structural studies on the mechanisms of aggregation and neurotoxicity.

Original languageEnglish
JournalBiochimie
Volume140
Pages (from-to)176-192
Number of pages17
ISSN0300-9084
DOIs
Publication statusPublished - 09.2017

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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