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Metal ions differentially influence the aggregation and deposition of Alzheimer's beta-amyloid on a solid template.
- Source :
-
Biochemistry [Biochemistry] 2007 May 22; Vol. 46 (20), pp. 6118-25. Date of Electronic Publication: 2007 Apr 25. - Publication Year :
- 2007
-
Abstract
- The abnormal deposition and aggregation of beta-amyloid (Abeta) on brain tissues are considered to be one of the characteristic neuropathological features of Alzheimer's disease (AD). Environmental conditions such as metal ions, pH, and cell membranes are associated with Abeta deposition and plaque formation. According to the amyloid cascade hypothesis of AD, the deposition of Abeta42 oligomers as diffuse plaques in vivo is an important earliest event, leading to the formation of fibrillar amyloid plaques by the further accumulation of soluble Abeta under certain environmental conditions. In order to characterize the effect of metal ions on amyloid deposition and plaque growth on a solid surface, we prepared a synthetic template by immobilizing Abeta oligomers onto a N-hydroxysuccinimide ester-activated solid surface. According to our study using ex situ atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FT-IR), and thioflavin T (ThT) fluorescence spectroscopy, Cu2+ and Zn2+ ions accelerated both Abeta40 and Abeta42 deposition but resulted only in the formation of "amorphous" aggregates. In contrast, Fe3+ induced the deposition of "fibrillar" amyloid plaques at neutral pH. Under mildly acidic environments, the formation of fibrillar amyloid plaques was not induced by any metal ion tested in this work. Using secondary ion mass spectroscopy (SIMS) analysis, we found that binding Cu ions to Abeta deposits on a solid template occurred by the possible reduction of Cu ions during the interaction of Abeta with Cu2+. Our results may provide insights into the role of metal ions on the formation of fibrillar or amorphous amyloid plaques in AD.
- Subjects :
- Amyloid beta-Peptides metabolism
Amyloid beta-Peptides ultrastructure
Cations, Divalent chemistry
Copper chemistry
Esters
Ferric Compounds chemistry
Hydrogen-Ion Concentration
Microscopy, Atomic Force
Peptide Fragments metabolism
Peptide Fragments ultrastructure
Plaque, Amyloid chemistry
Plaque, Amyloid metabolism
Spectrometry, Mass, Secondary Ion
Surface Properties
Zinc chemistry
Alzheimer Disease metabolism
Amyloid beta-Peptides chemistry
Metals, Heavy chemistry
Peptide Fragments chemistry
Succinimides chemistry
Succinimides metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 46
- Issue :
- 20
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 17455909
- Full Text :
- https://doi.org/10.1021/bi7000032