Copper and zinc mediated oligomerisation of A beta peptides
- Author(s)
- Ali, FE; Separovic, F; Barrow, CJ; Yao, SG; Barnham, KJ;
- Details
- Publication Year 2006-06,Volume 12,Issue #2,Page 153-164
- Journal Title
- INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
- Publication Type
- Journal Article
- Abstract
- The accumulation of senile plaques composed primarily of aggregated amyloid P-peptide (AD), 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 A beta 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 A beta peptide, A beta(1-16), were studied. The effect of Cu(2+) and Zn(2+) binding to A beta(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 Cu(2+) and Zn(2+) binding to A beta(1-16), with Cu(2+) showing a higher affinity for binding the peptide than Zn(2+).
- Publisher
- SPRINGER
- Keywords
- AMYLOID PRECURSOR PROTEIN; ALZHEIMERS-DISEASE; SELF-ASSOCIATION; BINDING MODES; IN-VITRO; AGGREGATION; NMR; DIFFUSION; PLAQUES; CU(II)
- Publisher's Version
- https://doi.org/10.1007/s10989-006-9012-9
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2006-06-01 12:00:00