The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
The Amyloid-β Peptide of Alzheimer’s Disease Binds Cu I in a Linear Bis-His Coordination Environment: Insight into a Possible Neuroprotective Mechanism for the Amyloid-β Peptide
Open accessAbstract
Oxidative stress has been suggested to contribute to neuronal apoptosis associated with Alzheimer's disease (AD). Copper may participate in oxidative stress through redox-cycling between its +2 and +1 oxidation states to generate reactive oxygen species (ROS). In vitro, copper binds to the amyloid-beta peptide of AD, and in vivo, copper is associated with amyloid plaques characteristic of AD. As a result, the AbetaCu(I) complex may be a critical reactant involved in ROS associated with AD etiology. To characterize the AbetaCu(I) complex, we have pursued X-ray absorption (XAS) and electron paramagnetic resonance (EPR) spectroscopy of AbetaCu(II) and AbetaCu(I) (produced by ascorbate reduction of AbetaCu(II)). The AbetaCu(II) complex Cu K-edge XAS spectrum is indicative of a square-planar Cu(II) center with mixed N/O ligation. Multiple scattering analysis of the extended X-ray absorption fine structure (EXAFS) data for AbetaCu(II) indicates that two of the ligands are imidazole groups of histidine ligands, indicating a (N(Im))(2)(N/O)(2) Cu(II) ligation sphere for AbetaCu(II). After reduction of the AbetaCu(II) complex with ascorbate, the edge region decreases in energy by approximately 4 eV. The X-ray absorption near-edge spectrum region of AbetaCu(I) displays an intense pre-edge feature at 8984.1(2) eV. EXAFS data fitting yielded a two-coordinate geometry, with two imidazole ligands coordinated to Cu(I) at 1.877(2) A in a linear geometry. Ascorbate reduction of AbetaCu(II) under inert atmosphere and subsequent air oxidation of AbetaCu(I) to regenerate AbetaCu(II) was monitored by low-temperature EPR spectroscopy. Slow reappearance of the AbetaCu(II) EPR signal indicates that O(2) oxidation of the AbetaCu(I) complex is kinetically sluggish and Abeta damage is occurring following reoxidation of AbetaCu(I) by O(2). Together, these results lead us to hypothesize that Cu(I) is ligated by His13 and His14 in a linear coordination environment in Alphabeta, that Abeta may be playing a neuroprotective role, and that metal-mediated oxidative damage of Abeta occurs over multiple redox cycles.
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Cites
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Amyloid-β Binds Cu 2+ in a Mononuclear Metal Ion Binding Site
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Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185
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“It has been reported that neurotoxic forms of amyloid β, Aβ (1–42), Aβ (1–40), and also Aβ (25–35) induced copper-mediated oxidation of ascorbate, whereas non-toxic Aβ (40–1) did not [110,111].”
BackgroundSmall Molecule Modulators of Copper-Induced Aβ Aggregation
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Atrián-Blasco, E., del Barrio, M., Faller, P., & Hureau, C. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b00740 · Cited by 62
Impact of N‐Truncated Aβ Peptides on Cu‐ and Cu(Aβ)‐Generated ROS: CuI Matters!
Esmieu, C., Ferrand, G., Borghesani, V., & Hureau, C. (2021) · Chemistry – A European Journal · doi:10.1002/chem.202003949 · Cited by 43
Prosdocimi, T., De Gioia, L., Zampella, G., & Bertini, L. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-015-1322-y · Cited by 32
Tomasello, M. F., Di Rosa, M. C., Naletova, I., Sciacca, M. F. M., Giuffrida, A., Maccarrone, G., & Attanasio, F. (2025) · Bioinorganic Chemistry and Applications · doi:10.1155/bca/4226220 · Cited by 3
“Te resulting Cu(I) cannot form complex with Semax but could form complex with a β , which is known to form relatively weak complex with Cu(I) [86–88].”
Metadata
- Authors
- Shearer, J., & Szalai, V. A.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2008-11-26
- Volume
- 130
- Issue
- 52
- Pages
- 17826-17835
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2001221518
- Cited by
- 189
- References
- 11
- FWCI
- 8.04
- Type
- journal article
- Language
- en
- Open access
- green
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