ArticleBiophysical journal2012
β-Amyloid (1-40) peptide interactions with supported phospholipid membranes: a single-molecule study.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Targeting soluble misfolded oligomers in anti-amyloid research.Nature reviews. Chemistry · 2026Review
- Advancing membrane biology: single-molecule approaches meet model membrane systems.BMB reports · 2025Review
- Cholesterol as a key player in amyloid β-mediated toxicity in Alzheimer's disease.Frontiers in molecular neuroscience · 2022Review
- Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders.Antioxidants (Basel, Switzerland) · 2021Review
- Single Molecule Characterization of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2021Review
- The F19W mutation reduces the binding affinity of the transmembrane AβRSC advances · 2021Article
- Single Molecule Measurements of the Accessibility of Molecular Surfaces.Frontiers in molecular biosciences · 2021Article
- GABA-A receptor modulating steroids in acute and chronic stress; relevance for cognition and dementia?Neurobiology of stress · 2020Article
- The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue β-amyloid peptides in biologically relevant model liposomes.Biochimica et biophysica acta. Biomembranes · 2018Article
- Membrane-Modulating Drugs can Affect the Size of Amyloid-βScientific reports · 2018Article
- Single-molecule photobleaching: Instrumentation and applications.Journal of biosciences · 2018Article
- Binding of protofibrillar Aβ trimers to lipid bilayer surface enhances Aβ structural stability and causes membrane thinning.Physical chemistry chemical physics : PCCP · 2017Article
- Article
- Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1-42) compared to Aβ(1-40).Scientific reports · 2017Article
- Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes.The Journal of biological chemistry · 2017Article
- Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?PLoS computational biology · 2017Article
- Lipid-Bilayer Dynamics Probed by a Carbon Dot-Phospholipid Conjugate.Biophysical journal · 2016Article
- The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol.Membranes · 2015Article
- Monitoring of single vesicle cytochrome-c release illuminates BAK as a novel target of Aβ oligomers.Biophysical journal · 2014Article
- Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies.Protein science : a publication of the Protein Society · 2014Review
Corrections and comments
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4 authors.
Funding
Abstract
Recent evidence supports the hypothesis that the oligomers formed by the β-amyloid peptide early in its aggregation process are neurotoxic and may feature in Alzheimer's disease. Although the mechanism underlying this neurotoxicity remains unclear, interactions of these oligomers with neuronal membranes are believed to be involved. Identifying the neurotoxic species is challenging because β-amyloid peptides form oligomers at very low physiological concentrations (nM), and these oligomers are highly heterogeneous and metastable. Here, we report the use of single-molecule imaging techniques to study the interactions between β-amyloid (1-40) peptides and supported synthetic model anionic lipid membranes. The evolution of the β-amyloid species on the membranes was monitored for up to several days, and the results indicate an initial tight, uniform, binding of β-amyloid (1-40) peptides to the lipid membranes, followed by oligomer formation in the membrane. At these low concentrations, the behavior at early times during the formation of small oligomers is interpreted qualitatively in terms of the two-state model proposed by H. W. Huang for the interaction between amphipathic peptides and membranes. However, the rate of oligomer formation in the membrane and their size are highly dependent on the concentrations of β-amyloid (1-40) peptides in aqueous solution, suggesting two different pathways of oligomer formation, which lead to drastically different species in the membrane and a departure from the two-state model as the concentration increases.
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Registered trials
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