ArticleBiochemistry2010
Simultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayers.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 52 citations in OpenAlex.
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAPBiophysical journal · 2020Article
- How Fluorescent Tags Modify Oligomer Size Distributions of the Alzheimer Peptide.Biophysical journal · 2019Article
- Computational modeling of amylin-induced calcium dysregulation in rat ventricular cardiomyocytes.Cell calcium · 2018Article
- Modeling the neuron as a nanocommunication system to identify spatiotemporal molecular events in neurodegenerative disease.International journal of nanomedicine · 2018Article
- Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.Scientific reports · 2016Article
- Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores.The Yale journal of biology and medicine · 2016Review
- A Kinetic Model for Cell Damage Caused by Oligomer Formation.Biophysical journal · 2015Article
- Single-cell screening of cytosolic [Ca(2+)] reveals cell-selective action by the Alzheimer's Aβ peptide ion channel.Cell stress & chaperones · 2015Article
- Single-molecule imaging reveals that small amyloid-β1-42 oligomers interact with the cellular prion protein (PrP(C)).Chembiochem : a European journal of chemical biology · 2014Article
- Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Chemical Society reviews · 2014Review
- 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
- Misfolding of amyloidogenic proteins and their interactions with membranes.Biomolecules · 2013Review
- A common landscape for membrane-active peptides.Protein science : a publication of the Protein Society · 2013Review
- Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments.Physical chemistry chemical physics : PCCP · 2013Article
- Alzheimer's disease: which type of amyloid-preventing drug agents to employ?Physical chemistry chemical physics : PCCP · 2013Review
- Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes.Biophysical journal · 2013Article
- Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Frontiers in physiology · 2013Article
- Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.PloS one · 2013Article
- β-Amyloid (1-40) peptide interactions with supported phospholipid membranes: a single-molecule study.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The extracellular senile plaques prevalent in brain tissue in Alzheimer's disease (AD) are composed of amyloid fibrils formed by the Abeta peptide. These fibrils have been traditionally believed to be featured in neurotoxicity; however, numerous recent studies provide evidence that cytotoxicity in AD may be associated with low-molecular weight oligomers of Abeta that associate with neuronal membranes and may lead to membrane permeabilization and disruption of the ion balance in the cell. The underlying mechanism leading to disruption of the membrane is the subject of many recent studies. Here we report the application of single-molecule optical detection, using fluorescently labeled human Alphabeta40, combined with membrane conductivity measurements, to monitor the interaction of single-oligomeric peptide structures with model planar black lipid membranes (BLMs). In a qualitative study, we show that the binding of Alphabeta to the membrane can be described by three distinctly different behaviors, depending on the Alphabeta monomer concentration. For concentrations much below 10 nM, there is uniform binding of monomers over the surface of the membrane with no evidence of oligomer formation or membrane permeabilization. Between 10 nM and a few hundred nanomolar, the uniform monomer binding is accompanied by the presence of peptide species ranging from dimers to small oligomers. The dimers are not found to permeabilize the membrane, but the larger oligomers lead to permeabilization with individual oligomers producing ion conductances of <10 pS/pore. At higher concentrations, perhaps beyond physiologically relevant concentrations, larger extended and dynamic structures are found with large conductances (hundreds of picosiemens), suggesting a major disruption of the membrane.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.