Amyloid β-Protein Dimers Rapidly Form Stable Synaptotoxic Protofibrils
Open accessAbstract
Nonfibrillar, water-soluble low-molecular weight assemblies of the amyloid β-protein (Aβ) are believed to play an important role in Alzheimer's disease (AD). Aqueous extracts of human brain contain Aβ assemblies that migrate on SDS-polyacrylamide gels and elute from size exclusion as dimers (∼8 kDa) and can block long-term potentiation and impair memory consolidation in the rat. Such species are detected specifically and sensitively in extracts of Alzheimer brain suggesting that SDS-stable dimers may be the basic building blocks of AD-associated synaptotoxic assemblies. Consequently, understanding the structure and properties of Aβ dimers is of great interest. In the absence of sufficient brain-derived dimer to facilitate biophysical analysis, we generated synthetic dimers designed to mimic the natural species. For this, Aβ(1-40) containing cysteine in place of serine 26 was used to produce disulphide cross-linked dimer, (AβS26C)2. Such dimers had no detectable secondary structure, produced an analytical ultracentrifugation profile consistent for an ∼8.6 kDa protein, and had no effect on hippocampal long-term potentiation (LTP). However, (AβS26C)2 aggregated more rapidly than either AβS26C or wild-type monomers and formed parastable β-sheet rich, thioflavin T-positive, protofibril-like assemblies. Whereas wild-type Aβ aggregated to form typical amyloid fibrils, the protofibril-like structures formed by (AβS26C)2 persisted for prolonged periods and potently inhibited LTP in mouse hippocampus. These data support the idea that Aβ dimers may stabilize the formation of fibril intermediates by a process distinct from that available to Aβ monomer and that higher molecular weight prefibrillar assemblies are the proximate mediators of Aβ toxicity.
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Soluble Aβ aggregates are more toxic than monomers or insoluble fibrils.
“Among these various forms, soluble Aβ aggregates are more toxic than monomers or insoluble fibrils; thus, reducing these soluble Aβ aggregates could represent a practical treatment approach in the early stages of AD [10,11,12].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [11]
The Discussion describes non-fibrillar, water-soluble Aβ as the principal mediators of neurotoxicity, and the Results show that soluble protofibrils inhibit synaptic plasticity. The paper does not directly compare their toxicity with that of monomers or insoluble mature fibrils, so the full comparative claim is not established. (LLM, conf=0.82)
Experimental — accuracy not yet measuredReducing soluble Aβ aggregates could represent a practical treatment approach in the early stages of AD.
“Among these various forms, soluble Aβ aggregates are more toxic than monomers or insoluble fibrils; thus, reducing these soluble Aβ aggregates could represent a practical treatment approach in the early stages of AD [10,11,12].”
From Treatment of Alzheimer’s Disease: Beyond Symptomatic Therapies (2023) · cites this paper as [11]
The Discussion (page unavailable) says therapeutic targeting of Aβ dimers remains attractive because it should prevent formation of toxic pre-fibrillar assemblies. This supports a possible treatment strategy, but the paper does not specify treatment in the early stages of AD or establish that broadly reducing soluble aggregates is practical. (LLM, conf=0.85)
Experimental — accuracy not yet measured
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- Authors
- O'Nuallain, B., Freir, D. B., Nicoll, A. J., Risse, E., Ferguson, N., Herron, C. E., Collinge, J., & Walsh, D. M.
- Affiliations
- University College Dublin (IE)
- MRC Prion Unit (GB)
- Corresponding author
- Walsh, Dominic M.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-10-27
- Volume
- 30
- Issue
- 43
- Pages
- 14411-14419
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2987723
- OpenAlex
- W2040863516
- Cited by
- 259
- References
- 48
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- FWCI
- 16.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
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- UCL Discovery (University College London) (submittedVersion)
- Research Repository UCD (University College Dublin) (submittedVersion, cc-by-nc-nd)
- Funders
- Health Research Board
- Science Foundation Ireland (0.8/1N.1/B2033)
- National Institutes of Health
- U.S. Public Health Service (IRO1AGO27443)
- National Institute on Aging (R01AG027443)
- 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
- amyloid-beta, protofibrils, Alzheimer's disease, synaptotoxicity, long-term potentiation, Aβ(1-40), protein aggregation, beta-sheet, hippocampus
- MeSH terms
- Amino Acid Sequence, Animals, Circular Dichroism, Cross-Linking Reagents, Drug Synergism, Electrophoresis, Polyacrylamide Gel, Electrophysiology, Light, Male, Mice, Inbred C57BL, Microscopy, Electron, Molecular Sequence Data, Neuronal Plasticity, Neurotoxins, Protein Conformation, Scattering, Radiation, Synapses, Ultracentrifugation, Amyloid beta-Peptides, Neurofibrillary Tangles, Dimerization, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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