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Neurotoxicity in Alzheimer’s disease: is covalently crosslinked Aβ responsible?

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Abstract

Alzheimer’s disease is the most common form of dementia in the elderly, and is characterised by extracellular amyloid plaques composed of the β-amyloid peptide (Aβ). However, disease progression has been shown to correlate more closely with the level of soluble Aβ oligomers. Recent evidence suggests that these oligomers are covalently crosslinked, possibly due to the interaction of Aβ with redox-active metal ions. These findings offer new avenues for the treatment and prevention of disease, by modulating metal binding or preventing the formation of neurotoxic Aβ oligomers.

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Authors and Affiliations

  1. Department of Pathology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, 3010, Australia

    Ryan Naylor & Kevin J. Barnham

  2. Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC, 3010, Australia

    Ryan Naylor & Andrew F. Hill

Authors
  1. Ryan Naylor
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  2. Andrew F. Hill
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  3. Kevin J. Barnham
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Correspondence to Kevin J. Barnham.

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Australian Society for Biophysics Special Issue: Metals and Membranes in Neuroscience.

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Naylor, R., Hill, A.F. & Barnham, K.J. Neurotoxicity in Alzheimer’s disease: is covalently crosslinked Aβ responsible?. Eur Biophys J 37, 265–268 (2008). https://doi.org/10.1007/s00249-007-0243-2

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  • DOI: https://doi.org/10.1007/s00249-007-0243-2

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