Metal Ions Differentially Influence the Aggregation and Deposition of Alzheimer's β-Amyloid on a Solid Template
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 reductio…
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In the presence of diamagnetic Zn2+ ions, the decrease in ThT fluorescence suggests the formation of non-fibrillar aggregates.
“In the presence of diamagnetic Zn2+ ions, although the effect is slightly lower than for Cu2+, the decrease in ThT fluorescence suggests the formation of non-fibrilar aggregates (see below),48”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [48]
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- Authors
- Ha, C., Ryu, J., & Park, C. B.
- Affiliations
- Korea Advanced Institute of Science and Technology (KR)
- Corresponding author
- Park, Chan Beum
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-04-25
- Volume
- 46
- Issue
- 20
- Pages
- 6118-6125
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2002330213
- Cited by
- 231
- References
- 3
- Citations by year
- 2026: 5 · 2025: 12 · 2024: 13 · 2023: 6 · 2022: 10 · 2021: 14 · 2020: 11 · 2019: 18 · 2018: 17 · 2017: 13 · 2016: 9 · 2015: 15 · 2014: 8 · 2013: 12 · 2012: 17
- FWCI
- 8.64
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Funders
- National Institutes of Health (1r21ag024114-01a2)
- National Institute on Aging (1R21AG024114-01A2)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- amyloid-beta, Alzheimer's disease, metal ions, amyloid fibril formation, amyloid plaque formation, copper ions, zinc ions, iron ions, Aβ40, amyloid-beta 42, amyloid fibrils, amorphous aggregates, pH effect, copper reduction
- MeSH terms
- Alzheimer Disease, Cations, Divalent, Copper, Esters, Ferric Compounds, Hydrogen-Ion Concentration, Peptide Fragments, Succinimides, Surface Properties, Zinc, Amyloid beta-Peptides, Microscopy, Atomic Force, Spectrometry, Mass, Secondary Ion, Metals, Heavy, Plaque, Amyloid
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