| Autor: |
Everett J; Institute for Science and Technology in Medicine, Keele University , Stoke-on-Trent, Staffordshire ST4 7QB, United Kingdom., Céspedes E, Shelford LR, Exley C, Collingwood JF, Dobson J, van der Laan G, Jenkins CA, Arenholz E, Telling ND |
| Jazyk: |
angličtina |
| Zdroj: |
Inorganic chemistry [Inorg Chem] 2014 Mar 17; Vol. 53 (6), pp. 2803-9. Date of Electronic Publication: 2014 Feb 21. |
| DOI: |
10.1021/ic402406g |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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