Evidence of Redox-Active Iron Formation Following Aggregation of Ferrihydrite and the Alzheimer鈥檚 Disease Peptide 尾-Amyloid

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• 作者：James Everett ; Eva C茅spedes ; Leigh R. Shelford ; Chris Exley ; Joanna F. Collingwood ; Jon Dobson ; Gerrit van der Laan ; Catherine A. Jenkins ; Elke Arenholz ; Neil D. Telling
• 刊名：Inorganic Chemistry
• 出版年：2014
• 出版时间：March 17, 2014
• 年：2014
• 卷：53
• 期：6
• 页码：2803-2809
• 全文大小：456K
• 年卷期：v.53,no.6(March 17, 2014)
• ISSN：1520-510X

文摘

Recent work has demonstrated increased levels of redox-active iron biominerals in Alzheimer鈥檚 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 尾-amyloid (A尾) and ferrihydrite, which is the ferric form taken when iron is stored in humans. We report that A尾 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 A尾 to induce the redox-active biominerals reported in AD tissue from natural iron precursors. Such interactions between A尾 and ferrihydrite shed light upon the processes of AD pathogenesis, while providing potential targets for future therapies.