The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State
Abstract
Aggregation of the β‐amyloid peptide (Aβ) to amyloid plaques is a key event in Alzheimer's disease. According to the amyloid‐cascade hypothesis, Aβ aggregates are toxic to neurons through the production of reactive oxygen species (ROS). Copper ions play an important role, because they are able to bind to Aβ and influence its aggregation properties. Moreover, Cu–Aβ is supposed to be directly involved in ROS production. To get a better understanding of these reactions, we measured the production of HO. and the redox potential of Cu–Aβ. The results were compared to other biological copper–peptide complexes in order to get an insight into the biological relevance. Cu–Aβ produced more HO. than the complex of copper with Asp‐Ala‐His‐Lys (Cu–DAHK), but less than with Gly‐His‐Lys (Cu–GHK). Cyclic voltammetry revealed that the order for reduction potential is Cu–GHK>Cu–Aβ>Cu–DAHK, but for the oxidation potential the order is reversed. Thus, easier copper redox cycling correlated to higher HO. production. The copper complex of the form Aβ1–42 showed a HO. production five‐times higher than that of the form Aβ1–40. Time‐dependence and aggregation studies suggest that an aggregation intermediate is responsible for this increased HO. production.
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Cites
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Free Radicals in Biology and Medicine
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Cited by
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
Self-citationNguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Self-citationBioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530
Self-citationThe chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease
Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 400
Metadata
- Authors
- Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P.
- Venue
- ChemBioChem
- Publisher
- Wiley
- Published
- 2007-07-10
- Volume
- 8
- Issue
- 11
- Pages
- 1317-1325
- ISSN
- 1439-4227 (ISSN-L)
- 1439-7633
- OpenAlex
- W2113950441
- Cited by
- 270
- References
- 9
- FWCI
- 7.71
- Type
- journal article
- Language
- en
- Open access
- closed
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- Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007). Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State. ChemBioChem. https://doi.org/10.1002/cbic.200700111
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