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Copper and zinc mediated oligomerisation of Aß peptides

Ali, Feda E., Separovic, Frances, Barrow, Colin J., Yao, Shenggen and Barnham, Kevin J. 2006, Copper and zinc mediated oligomerisation of Aß peptides, International journal of peptide research and therapeutics, vol. 12, no. 2, pp. 153-164.

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Title Copper and zinc mediated oligomerisation of Aß peptides
Author(s) Ali, Feda E.
Separovic, Frances
Barrow, Colin J.
Yao, Shenggen
Barnham, Kevin J.
Journal name International journal of peptide research and therapeutics
Volume number 12
Issue number 2
Start page 153
End page 164
Publisher Springer Netherlands
Place of publication Amsterdam, Netherlands
Publication date 2006-06
ISSN 1573-3149
1573-3904
Keyword(s) Aβ
amyloid β peptide
Alzheimer's disease
metal binding
oligomerisation
copper
zinc
Summary The accumulation of senile plaques composed primarily of aggregated amyloid β-peptide (Aβ), is the major characteristic of Alzheimer’s disease. Many studies correlate plaque accumulation and the presence of metal ions, particularly copper and zinc. The metal binding sites of the amyloid Aβ peptide of Alzheimer’s disease are located in the N-terminal region of the full-length peptide. In this work, the interactions with metals of a model peptide comprising the first 16 amino acid residues of the amyloid Aβ peptide, Aβ(1–16), were studied. The effect of Cu2+ and Zn2+ binding to Aβ(1–16) on peptide structure and oligomerisation are reported. The results of ESI-MS, gel filtration chromatography and NMR spectroscopy demonstrated formation of oligomeric complexes of the peptide in the presence of the metal ions and revealed the stoichiometry of Cu2+ and Zn2+ binding to Aβ(1–16), with Cu2+ showing a higher affinity for binding the peptide than Zn2+.
Language eng
Field of Research 030406 Proteins and Peptides
110106 Medical Biochemistry: Proteins and Peptides (incl Medical Proteomics)
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2006, Springer Science+Business Media
Persistent URL http://hdl.handle.net/10536/DRO/DU:30019482

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