Neurotoxicity of Alzheimer’s disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio
Open accessAbstract
The amyloid peptides Aβ(40) and Aβ(42) of Alzheimer's disease are thought to contribute differentially to the disease process. Although Aβ(42) seems more pathogenic than Aβ(40), the reason for this is not well understood. We show here that small alterations in the Aβ(42):Aβ(40) ratio dramatically affect the biophysical and biological properties of the Aβ mixtures reflected in their aggregation kinetics, the morphology of the resulting amyloid fibrils and synaptic function tested in vitro and in vivo. A minor increase in the Aβ(42):Aβ(40) ratio stabilizes toxic oligomeric species with intermediate conformations. The initial toxic impact of these Aβ species is synaptic in nature, but this can spread into the cells leading to neuronal cell death. The fact that the relative ratio of Aβ peptides is more crucial than the absolute amounts of peptides for the induction of neurotoxic conformations has important implications for anti-amyloid therapy. Our work also suggests the dynamic nature of the equilibrium between toxic and non-toxic intermediates.
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The increased amyloid beta 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates.
“The increased Aβ 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates [28,42,43]”
From Selective suppression of oligodendrocyte-derived amyloid beta rescues neuronal dysfunction in Alzheimer’s disease (2024) · cites this paper as [43]
The Abstract says a minor increase in the Aβ42:Aβ40 ratio stabilizes toxic oligomeric species, supporting the proposed link between the ratio and soluble aggregates. The paper studies Aβ mixtures and neuronal effects, however; it does not establish an increased ratio or a high proportion of soluble aggregates in oligodendrocytes. (LLM, conf=0.86)
Experimental — accuracy not yet measuredAβ40 is present in larger amounts in the brain, yet Aβ42 is more neurotoxic and has a higher tendency to aggregate.
“Aβ40 is present in larger amounts in the brain, yet Aβ42 is more neurotoxic and has a higher tendency to aggregate.8–11”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ<sub>42</sub>Peptide (2012) · cites this paper as [10]
The Introduction says Aβ40 is the major species in serum, cerebrospinal fluid, and cell-culture supernatants, with Aβ42 detected at about tenfold lower levels; it does not establish their relative amounts in brain tissue. The Introduction also describes faster Aβ42 aggregation, and the Abstract and results support its greater toxic potential, while emphasizing that toxicity depends on the Aβ42:Aβ40 ratio. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe longer and more hydrophobic Aβ42 isoform has a higher tendency to generate neurotoxic oligomeric species than Aβ40.
“the longer and more hydrophobic Aβ42 isoform has a higher tendency to generate neurotoxic oligomeric species.9,10”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [10]
The ‘Long-term cellular toxicity of Aβ mixtures’ section reports neurotoxicity from Aβ42 alone but not Aβ40 alone; the discussion links Aβ42-rich preparations to toxic intermediates. This supports the comparative tendency, but our copy does not establish that Aβ42’s greater hydrophobicity explains it, and emphasizes the importance of the Aβ42:Aβ40 ratio. (LLM, conf=0.85)
Experimental — accuracy not yet measuredAβ42 is more neurotoxic and has a higher tendency to aggregate than Aβ40.
“Although Aβ40 is present in larger amounts in the brain, Aβ42 was found to be more neurotoxic and have a higher tendency to aggregate.4,5”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [5]
Aβ42 peptide is more prone to form neurotoxic soluble Aβ oligomers than the Aβ40 peptide.
“Although it was shown in previous studies9,10,21 that the Aβ42 peptide is more prone to form neurotoxic soluble Aβ oligomers than the Aβ40 peptide”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [10]
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- Authors
- Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., Braeken, D., Callewaert, G., Bartic, C., D'Hooge, R., Martins, I. C., Rousseau, F., Schymkowitz, J., & De Strooper, B.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Vrije Universiteit Brussel (BE)
- Rega Institute for Medical Research (BE)
- University of Twente (NL)
- IMEC (BE)
- Corresponding author
- Schymkowitz, Joost
- ORCID
- Venue
- The EMBO Journal
- Published
- 2010-09-03
- Volume
- 29
- Issue
- 19
- Pages
- 3408-3420
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2957213
- OpenAlex
- W1966694507
- Cited by
- 532
- References
- 61
- Citations by year
- 2026: 16 · 2025: 23 · 2024: 36 · 2023: 39 · 2022: 27 · 2021: 39 · 2020: 32 · 2019: 33 · 2018: 31 · 2017: 35 · 2016: 48 · 2015: 31 · 2014: 30 · 2013: 42 · 2012: 43
- FWCI
- 24.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- VU Research Portal (publishedVersion)
- University of Twente Research Information (publishedVersion, other-oa)
- Lirias (submittedVersion)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- University of Twente Research Information (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- European Commission (200611)
- Fonds Wetenschappelijk Onderzoek (P6/43)
- Vlaamse regering
- 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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta, Aβ42/Aβ40 ratio, neurotoxicity, oligomeric intermediates, fibril morphology, synaptic dysfunction, neuronal cell death, anti-amyloid therapy, peptide mixtures
- MeSH terms
- Alzheimer Disease, Analysis of Variance, Animals, Biophysics, Fluorescent Dyes, Humans, Kinetics, Microelectrodes, Neurons, Peptide Fragments, Protein Binding, Thiazoles, Amyloid beta-Peptides, Spectroscopy, Fourier Transform Infrared, Patch-Clamp Techniques, Microscopy, Electron, Transmission, Mice, Benzothiazoles, Plaque, Amyloid
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