Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer's disease peptide β-amyloid (1–42)
Abstract
For decades, a link between increased levels of iron and areas of Alzheimer’s disease (AD) pathology has been recognized, including AD lesions comprised of the peptide b-amyloid (Ab). Despite many observations of this association, the relationship between Ab and iron is poorly understood. Using X-ray microspectroscopy, X-ray absorption spectroscopy, electron microscopy and spectrophotometric iron(II) quantification techniques, we examine the interaction between Ab(1–42) and synthetic iron(III), reminiscent of ferric iron stores in the brain. We report Ab to be capable of accumulating iron(III) within amyloid aggregates, with this process resulting in Ab-mediated reduction of iron(III) to a redox-active iron(II) phase. Additionally, we show that the presence of aluminium increases the reductive capacity of Ab, enabling the redox cycling of the iron. These results demonstrate the ability of Ab to accumulate iron, offering an explanation for previously observed local increases in iron concentration associated with AD lesions. Furthermore, the ability of iron to form redox-active iron phases from ferric precursors provides an origin both for the redox-active iron previously witnessed in AD tissue, and the increased levels of oxidative stress characteristic of AD. These interactions between Ab and iron deliver valuable insights into the process of AD progression, which may ultimately providemore »
- Authors:
-
- Keele Univ., Stoke-on-Trent, Staffordshire (United Kingdom). Inst. for Science and Technology in Medicine
- Univ. of Exeter (United Kingdom). College of Engineering, Mathematics and Physical Sciences
- Keele Univ., Stoke-on-Trent, Staffordshire (United Kingdom). The Birchall Centre. Lennard-Jones Labs.
- Univ. of Warwick, Coventry (United Kingdom). School of Engineering
- Univ. of Florida, Gainesville, FL (United States). J. Crayton Pruitt Family Dept. of Biomedical Engineering; Univ. of Florida, Gainesville, FL (United States). Dept. of Materials Science and Engineering
- Science and Technology Facilities Council (STFC), Oxford (United Kingdom). Diamond Light Source, Ltd. Magnetic Spectroscopy Group
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Advanced Light Source (ALS)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- OSTI Identifier:
- 1625586
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Journal of the Royal Society Interface
- Additional Journal Information:
- Journal Volume: 11; Journal Issue: 95; Journal ID: ISSN 1742-5689
- Publisher:
- The Royal Society
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Science & Technology - Other Topics; chemical biology; biophysics; biochemistry; Alzheimer’s disease; b-amyloid, wu¨stite; redox; X-ray absorption
Citation Formats
Everett, J., Céspedes, E., Shelford, L. R., Exley, C., Collingwood, J. F., Dobson, J., van der Laan, G., Jenkins, C. A., Arenholz, E., and Telling, N. D. Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer's disease peptide β-amyloid (1–42). United States: N. p., 2014.
Web. doi:10.1098/rsif.2014.0165.
Everett, J., Céspedes, E., Shelford, L. R., Exley, C., Collingwood, J. F., Dobson, J., van der Laan, G., Jenkins, C. A., Arenholz, E., & Telling, N. D. Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer's disease peptide β-amyloid (1–42). United States. https://doi.org/10.1098/rsif.2014.0165
Everett, J., Céspedes, E., Shelford, L. R., Exley, C., Collingwood, J. F., Dobson, J., van der Laan, G., Jenkins, C. A., Arenholz, E., and Telling, N. D. Fri .
"Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer's disease peptide β-amyloid (1–42)". United States. https://doi.org/10.1098/rsif.2014.0165. https://www.osti.gov/servlets/purl/1625586.
@article{osti_1625586,
title = {Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer's disease peptide β-amyloid (1–42)},
author = {Everett, J. and Céspedes, E. and Shelford, L. R. and Exley, C. and Collingwood, J. F. and Dobson, J. and van der Laan, G. and Jenkins, C. A. and Arenholz, E. and Telling, N. D.},
abstractNote = {For decades, a link between increased levels of iron and areas of Alzheimer’s disease (AD) pathology has been recognized, including AD lesions comprised of the peptide b-amyloid (Ab). Despite many observations of this association, the relationship between Ab and iron is poorly understood. Using X-ray microspectroscopy, X-ray absorption spectroscopy, electron microscopy and spectrophotometric iron(II) quantification techniques, we examine the interaction between Ab(1–42) and synthetic iron(III), reminiscent of ferric iron stores in the brain. We report Ab to be capable of accumulating iron(III) within amyloid aggregates, with this process resulting in Ab-mediated reduction of iron(III) to a redox-active iron(II) phase. Additionally, we show that the presence of aluminium increases the reductive capacity of Ab, enabling the redox cycling of the iron. These results demonstrate the ability of Ab to accumulate iron, offering an explanation for previously observed local increases in iron concentration associated with AD lesions. Furthermore, the ability of iron to form redox-active iron phases from ferric precursors provides an origin both for the redox-active iron previously witnessed in AD tissue, and the increased levels of oxidative stress characteristic of AD. These interactions between Ab and iron deliver valuable insights into the process of AD progression, which may ultimately provide targets for disease therapies.},
doi = {10.1098/rsif.2014.0165},
journal = {Journal of the Royal Society Interface},
number = 95,
volume = 11,
place = {United States},
year = {Fri Jun 06 00:00:00 EDT 2014},
month = {Fri Jun 06 00:00:00 EDT 2014}
}
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