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.

Attached Files
Name Description MIMEType Size Downloads

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)
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)
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
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
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 24 times in TR Web of Science
Scopus Citation Count Cited 26 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 408 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Wed, 16 Sep 2009, 09:26:39 EST by Rachael Mackenzie

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.