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Copper and zinc mediated oligomerisation of Aß peptides

journal contribution
posted on 2006-06-01, 00:00 authored by F Ali, F Separovic, Colin BarrowColin Barrow, S Yao, K Barnham
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+.

History

Journal

International journal of peptide research and therapeutics

Volume

12

Issue

2

Pagination

153 - 164

Publisher

Springer Netherlands

Location

Amsterdam, Netherlands

ISSN

1573-3149

eISSN

1573-3904

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2006, Springer Science+Business Media