Stabilization of Neurotoxic Soluble β-Sheet-Rich Conformations of the Alzheimer's Disease Amyloid-β Peptide
Open accessAbstract
An emerging paradigm for degenerative diseases associated with protein misfolding, such as Alzheimer's disease, is the formation of a toxic species due to structural transitions accompanied by oligomerization. Increasingly, the focus in Alzheimer's disease is on soluble oligomeric forms of the amyloid-beta peptide (Abeta) as the potential toxic species. Using a variety of methods, we have analyzed how sodium dodecyl sulphate (SDS) modulates the folding of Abeta40 and 42 and found that submicellar concentrations of SDS solubilize Abeta and induce structural transitions. Under these conditions, Abeta40 and 42 are interconverting oligomeric ensembles with a predominantly beta-sheet structure. The Abeta42 soluble oligomers form beta-sheet structures more readily and have increased stability compared with Abeta40 under identical conditions. The presence of added Cu(2+) significantly promotes and stabilizes the formation of the soluble oligomeric beta-sheet structures but these structures are nonamyloidogenic. In contrast, in the absence of added Cu(2+), these beta-sheet oligomers possess the hallmarks of amyloidogenic structures. These SDS-induced beta-sheet forms of Abeta, both in the presence and absence of Cu(2+), are toxic to neuronal cells.
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Metal ions are able to stabilize the soluble Aβ42 oligomers and thus partially inhibit the Aβ42 aggregation.
“These results suggest that metal ions are able to stabilize the soluble Aβ42 oligomers and thus partially inhibit the Aβ42 aggregation.89”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [89]
The Conclusion (page unavailable) says Cu2+ promotes the formation and stability of soluble Aβ oligomers, supporting the stabilization part for copper. It does not report that metal ions generally partially inhibit Aβ42 aggregation; the Discussion instead describes increased aggregation under the study conditions. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe 48 h total incubation leads to mature Aβ42 fibrils, as observed by TEM, while the Western blot shows the presence of higher order Aβ42 oligomers, likely due to an assembly-disassembly equilibrium that is established for mature Aβ fibrils.
“The 48 h total incubation leads to mature Aβ42 fibrils, as observed by TEM (Figure 10, panel a) while the Western blot shows the presence of higher order Aβ42 oligomers (Figure 10, lane a), likely due to an assembly-disassembly equilibrium that is established for mature Aβ fibrils.89–91”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [89]
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- Authors
- Tew, D. J., Bottomley, S. P., Smith, D. P., Ciccotosto, G. D., Babon, J., Hinds, M. G., Masters, C. L., Cappai, R., & Barnham, K. J.
- Affiliations
- Mental Health Research Institute (AU)
- Monash University (AU)
- Walter and Eliza Hall Institute of Medical Research (AU)
- Corresponding author
- Barnham, Kevin J.
- ORCID
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 2008-04
- Volume
- 94
- Issue
- 7
- Pages
- 2752-2766
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC2267149
- OpenAlex
- W1971525444
- Cited by
- 93
- References
- 63
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 5 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 4 · 2019: 4 · 2018: 6 · 2017: 6 · 2016: 4 · 2015: 2 · 2014: 1 · 2013: 7 · 2012: 9
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- SHURA (Sheffield Hallam University Research Archive) (Sheffield Hallam University) (submittedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta, Alzheimer's disease, soluble oligomers, β-sheet conformation, sodium dodecyl sulfate, protein misfolding, copper(II) ions, neurotoxicity, Aβ40, amyloid-beta 42, structural phase transition
- MeSH terms
- Animals, Cell Survival, Cells, Cultured, Computer Simulation, Dose-Response Relationship, Drug, Models, Chemical, Models, Molecular, Neurons, Neurotoxins, Structure-Activity Relationship, Amyloid beta-Peptides, Mice
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