Publication
Article Metrics
Citations
Online attention
Evidence of Redox-Active Iron Formation Following Aggregation of Ferrihydrite and the Alzheimers Disease Peptide β-Amyloid
Authors:
James
Everett
(Keele University)
,
Eva
Céspedes
(Keele University)
,
Leigh
Shelford
(University of Exeter)
,
Chris
Exley
(Keele University)
,
Joanna
Collingwood
(Warwick University)
,
Jon
Dobson
(Keele University)
,
Gerrit
Van Der Laan
(Diamond Light Source)
,
Catherine A.
Jenkins
(Lawrence Berkeley National Laboratory)
,
Elke
Arenholz
(Lawrence Berkeley National Laboratory)
,
Neil
Telling
(Keele University)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Inorganic Chemistry
, VOL 53 (6)
, PAGES 2803−2809
State:
Published (Approved)
Published:
February 2014
Diamond Proposal Number(s):
7670
,
8731

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 Fe2+ 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.
Journal Keywords: Ferrihydrite; Iron; Alzheimer's Disease; Redox-Active; Amyloid Peptide
Subject Areas:
Medicine
Instruments:
I10-Beamline for Advanced Dichroism
Other Facilities: ALS SLS