Everett, J ORCID: https://orcid.org/0000-0002-1864-9700, Céspedes, E, Shelford, LR, Exley, C ORCID: https://orcid.org/0000-0002-5116-7607, Collingwood, JF, Dobson, J, van der Laan, G, Jenkins, CA, Arenholz, E and Telling, ND ORCID: https://orcid.org/0000-0002-2683-5546 (2014) Evidence of redox-active iron formation following aggregation of ferrihydrite and the Alzheimer's disease peptide β-amyloid. Inorganic Chemistry, 53 (6). 2803 - 2809.

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Abstract

Recent work has demonstrated increased levels of redox-active iron biominerals in Alzheimer's disease (AD) tissue. However, the origin, nature, and role of iron in AD pathology remains unclear. Using X-ray absorption, X-ray microspectroscopy, and electron microscopy techniques, we examined interactions between the AD peptide β-amyloid (Aβ) and ferrihydrite, which is the ferric form taken when iron is stored in humans. We report that Aβ is capable of reducing ferrihydrite to a pure iron(II) mineral where antiferromagnetically ordered Fe(2+) cations occupy two nonequivalent crystal symmetry sites. Examination of these iron(II) phases following air exposure revealed a material consistent with the iron(II)-rich mineral magnetite. These results demonstrate the capability of Aβ to induce the redox-active biominerals reported in AD tissue from natural iron precursors. Such interactions between Aβ and ferrihydrite shed light upon the processes of AD pathogenesis, while providing potential targets for future therapies.

Item Type: Article
Additional Information: This article can be accessed from the publishers at https://pubs.acs.org/doi/10.1021/ic402406g
Subjects: Q Science > Q Science (General)
Q Science > QH Natural history
R Medicine > R Medicine (General)
Divisions: Faculty of Medicine and Health Sciences > School of Pharmacy and Bioengineering
Related URLs:
Depositing User: Symplectic
Date Deposited: 07 Jul 2020 13:51
Last Modified: 07 Jul 2020 13:51
URI: https://eprints.keele.ac.uk/id/eprint/8349

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