Aβ-mediated ROS production by Cu ions: Structural insights, mechanisms and relevance to Alzheimer's disease
Abstract
Metal ions are involved in Alzheimer's disease (AD) via their ability to induce aggregation of amyloidogenic peptide and production of Reactive Oxygen Species (ROS), two key events in the development of the pathology. Here, we review very recent results concerning the coordination of Cu(I) and Cu(II) ion to the amyloid-beta peptide, the one encountered in AD. Implications of these structural data for the redox chemistry of the Cu(I/II)-Abeta couple are discussed. The different pathways for the ROS generation by the Cu(I/II)-Abeta species are described. In the more relevant one, reduction of dioxygen is realized by a two-electron process involving two Cu(I) in close vicinity, while the production of the hydroxyl radical from hydrogen peroxide is less constrained. A brief summary of how the Abeta peptide is oxidised during the ROS production is also given. Lastly, the pro- vs. anti-oxidant properties of Abeta are commented on.
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Metal ions promote Aβ aggregation and formation of reactive oxygen species and lead to oxidative stress.
“For example, it was shown that that metal ions promote Aβ aggregation,16,17 as well as formation of reactive oxygen species (ROS) and lead to oxidative stress.18–20”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [18]
These metal ions lead to formation of reactive oxygen species (ROS) and oxidative stress.
“as well as lead to formation of reactive oxygen species (ROS) and oxidative stress.3,26–31,33–36”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [35]
Copper, iron, and zinc ions affect Aβ aggregation and lead to formation of reactive oxygen species.
“These metal ions have been shown to affect Aβ aggregation, as well as lead to the formation of reactive oxygen species (ROS).12−16”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [14]
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- Authors
- Hureau, C., & Faller, P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Hureau, Christelle
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 91
- Issue
- 10
- Pages
- 1212-1217
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2020526702
- Cited by
- 259
- References
- 83
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 11 · 2023: 7 · 2022: 7 · 2021: 12 · 2020: 13 · 2019: 15 · 2018: 17 · 2017: 23 · 2016: 19 · 2015: 10 · 2014: 17 · 2013: 16 · 2012: 31
- FWCI
- 16.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- amyloid-beta, copper ions, reactive oxygen species, Alzheimer's disease, copper coordination, dioxygen reduction, hydroxyl radicals, hydrogen peroxide, metal-peptide interactions, antioxidant activity
- MeSH terms
- Alzheimer Disease, Animals, Copper, Humans, Models, Biological, Signal Transduction, Amyloid beta-Peptides, Reactive Oxygen Species
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