Metal-catalyzed oxidative damage and oligomerization of the amyloid-β peptide of Alzheimer’s disease

Ali, Feda E. A., Barnham, Kevin J., Barrow, Colin J. and Separovic, Frances 2004, Metal-catalyzed oxidative damage and oligomerization of the amyloid-β peptide of Alzheimer’s disease, Australian journal of chemistry, vol. 57, no. 6, pp. 511-518.


Title Metal-catalyzed oxidative damage and oligomerization of the amyloid-β peptide of Alzheimer’s disease
Author(s) Ali, Feda E. A.
Barnham, Kevin J.
Barrow, Colin J.
Separovic, Frances
Journal name Australian journal of chemistry
Volume number 57
Issue number 6
Start page 511
End page 518
Total pages 8
Publisher CSIRO Publishing
Place of publication Collingwood, Vic.
Publication date 2004
ISSN 0004-9425
1445-0038
Summary The most common form of dementia in old age is Alzheimer’s disease (AD). The presence in the brain of senile plaque is the major pathological marker of AD. The plaques are primarily composed of aggregated amyloid-β peptide (Aβ). Aβ is a 40–42 amino acid peptide that is a proteolytic product derived from the β-amyloid precursor protein. The function of Aβ and the exact mechanism of Aβ aggregation and neurotoxicity are unclear. However, metal coordination by Aβ plays an important role in inducing aggregation and the generation of reactive oxygen species, which appears to be at least partially responsible for Aβ neurotoxicity. In this review we examine the role of copper and zinc ions in Aβ neurotoxicity, especially with regards to the generation of free radicals. We discuss the role of copper or zinc ions in oxidative damage and Aβ conformational changes and the relationship of these metals to AD.
Language eng
Field of Research 030499 Medicinal and Biomolecular Chemistry not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2004, CSIRO
Persistent URL http://hdl.handle.net/10536/DRO/DU:30023802

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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