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Identification of neurotoxic cross-linked amyloid-β dimers in the Alzheimer's brain

Journal article
Authors Gunnar Brinkmalm
W. Hong
Z. Wang
W. Liu
T. T. O'Malley
X. Sun
M. P. Frosch
D. J. Selkoe
Erik Portelius
Henrik Zetterberg
Kaj Blennow
D. M. Walsh
Published in Brain
Volume 142
Issue 5
Pages 1441-1457
ISSN 0006-8950
Publication year 2019
Published at Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry
Pages 1441-1457
Language en
Keywords amyloid-β-protein, human neurons, long-term potentiation, mass spectrometry, video microscopy
Subject categories Neurosciences


The primary structure of canonical amyloid-β-protein was elucidated more than 30 years ago, yet the forms of amyloid-β that play a role in Alzheimer's disease pathogenesis remain poorly defined. Studies of Alzheimer's disease brain extracts suggest that amyloid-β, which migrates on sodium dodecyl sulphate polyacrylamide gel electrophoresis with a molecular weight of ∼7 kDa (7kDa-Aβ), is particularly toxic; however, the nature of this species has been controversial. Using sophisticated mass spectrometry and sensitive assays of disease-relevant toxicity we show that brain-derived bioactive 7kDa-Aβ contains a heterogeneous mixture of covalently cross-linked dimers in the absence of any other detectable proteins. The identification of amyloid-β dimers may open a new phase of Alzheimer's research and allow a better understanding of Alzheimer's disease, and how to monitor and treat this devastating disorder. Future studies investigating the bioactivity of individual dimers cross-linked at known sites will be critical to this effort. © The Author(s) (2019). Published by Oxford University Press on behalf of the Guarantors of Brain. All rights reserved. For permissions, please email:

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