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Biochimie. 2017 Sep;140:176-192. doi: 10.1016/j.biochi.2017.07.011. Epub 2017 Jul 25.

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

Author information

1
Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga, Latvia. Electronic address: aleksis@osi.lv.
2
Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga, Latvia.
3
Department of Neuro-/Pathology, Translational Neurodegeneration Research and Neuropathology Lab, University of Oslo (UiO) & Oslo University Hospital (OUS), Norway; LIED, University of Lübeck Uzl, Germany; Leibniz-Institute of Plant Biochemistry (IPB), Halle, Germany.
4
Department of Physical Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga, Latvia; Department of Neurobiology, Care Sciences and Society, Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, Stockholm, Sweden.

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.

KEYWORDS:

Aggregation mechanism; Alzheimer's disease; Amyloid structure; Amyloid-β peptide; Neurotoxicity

PMID:
28751216
DOI:
10.1016/j.biochi.2017.07.011
[Indexed for MEDLINE]

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