ArticleFrontiers in physiology2013
Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.
Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Spontaneous Insertion of Aβ42 Dimers but Not Monomers into a Cholesterol-Rich Lipid Bilayer.ACS chemical neuroscience · 2026Article
- Membrane-assisted Aβ40 aggregation pathways.Cell reports. Physical science · 2025Article
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Membrane-assisted Aβ40 aggregation pathways.bioRxiv : the preprint server for biology · 2024Article
- Measuring the Size and Spontaneous Fluctuations of Amyloid Aggregates with Fluorescence Correlation Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane.Biophysical journal · 2020Article
- His6, His13, and His14 residues in Aβ 1-40 peptide significantly and specifically affect oligomeric equilibria.Scientific reports · 2019Article
- Dopamine transporter forms stable dimers in the live cell plasma membrane in a phosphatidylinositol 4,5-bisphosphate-independent manner.The Journal of biological chemistry · 2019Article
- Single-molecule photobleaching: Instrumentation and applications.Journal of biosciences · 2018Article
- Injected Amyloid Beta in the Olfactory Bulb Transfers to Other Brain Regions via Neural Connections in Mice.Molecular neurobiology · 2018Article
- The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Journal of Alzheimer's disease : JAD · 2018Review
- Dietary arachidonic acid increases deleterious effects of amyloid-β oligomers on learning abilities and expression of AMPA receptors: putative role of the ACSL4-cPLAAlzheimer's research & therapy · 2017Article
- Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at Atomic Level.Biophysical journal · 2017Article
- Glucose directs amyloid-beta into membrane-active oligomers.Physical chemistry chemical physics : PCCP · 2017Article
- Downregulation of RBO-PI4KIIIα Facilitates AβThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Effect of amyloids on the vesicular machinery: implications for somatic neurotransmission.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Acta neuropathologica · 2015Review
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Amyloid beta (Aβ) is an extracellular 39-43 residue long peptide present in the mammalian cerebrospinal fluid, whose aggregation is associated with Alzheimer's disease (AD). Small oligomers of Aβ are currently thought to be the key to toxicity. However, it is not clear why the monomers of Aβ are non-toxic, and at what stage of aggregation toxicity emerges. Interactions of Aβ with cell membranes is thought to be the initiator of toxicity, but membrane binding studies with different preparations of monomers and oligomers have not settled this issue. We have earlier found that thermodynamically stable Aβ monomers emerge spontaneously from oligomeric mixtures upon long term incubation in physiological solutions (Nag et al., 2011). Here we show that the membrane-affinity of these stable Aβ monomers is much lower than that of a mixture of monomers and small oligomers (containing dimers to decamers), providing a clue to the emergence of toxicity. Fluorescently labeled Aβ40 monomers show negligible binding to cell membranes of a neuronal cell line (RN46A) at physiological concentrations (250 nM), while oligomers at the same concentrations show strong binding within 30 min of incubation. The increased affinity most likely does not require any specific neuronal receptor, since this difference in membrane-affinity was also observed in a somatic cell-line (HEK 293T). Similar results are also obtained for Aβ42 monomers and oligomers. Minimal amount of cell death is observed at these concentrations even after 36 h of incubation. It is likely that membrane binding precedes subsequent slower toxic events induced by Aβ. Our results (a) provide an explanation for the non-toxic nature of Aβ monomers, (b) suggest that Aβ toxicity emerges at the initial oligomeric phase, and (c) provide a quick assay for monitoring the benign-to-toxic transformation of Aβ.
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