ArticleThe Journal of biological chemistry2014
The mechanism of membrane disruption by cytotoxic amyloid oligomers formed by prion protein(106-126) is dependent on bilayer composition.
Article in The Journal of biological chemistry, 2014. 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, 73 citations in OpenAlex.
- Toxic mechanisms of amyloid oligomers and therapeutic strategies.Protein science : a publication of the Protein Society · 2026Review
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation.Membranes · 2025Article
- Comparative Effects ofJournal of arthropod-borne diseases · 2023Article
- Imaging Amyloid-β Membrane Interactions: Ion-Channel Pores and Lipid-Bilayer Permeability in Alzheimer's Disease.Angewandte Chemie (International ed. in English) · 2023Review
- Imaging Amyloid-β Membrane Interactions: Ion-Channel Pores and Lipid-Bilayer Permeability in Alzheimer's Disease.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Review
- Cholesterol and its reciprocal association with prion infection.Cell and tissue research · 2023Review
- Spectral Phasor Analysis of Nile Red Identifies Membrane Microenvironment Changes in the Presence of Amyloid Peptides.Cell biochemistry and biophysics · 2023Article
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- Peptide Aggregation Induced Immunogenic Rupture (PAIIR).Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Controlled and Selective Photo-oxidation of Amyloid-β Fibrils by OligomericACS applied materials & interfaces · 2022Article
- What is the role of lipids in prion conversion and disease?Frontiers in molecular neuroscience · 2022Review
- Effects of the Hydrophilic N-Terminal Region on Aβ-Mediated Membrane Disruption.The journal of physical chemistry. B · 2021Article
- Natural Compound from Olive Oil Inhibits S100A9 Amyloid Formation and Cytotoxicity: Implications for Preventing Alzheimer's Disease.ACS chemical neuroscience · 2021Article
- 3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography.Chemical science · 2021Article
- Viroporins vs. Other Pore-Forming Proteins: What Lessons Can We Take?Frontiers in chemistry · 2021Review
- Imaging Flow Cytometry Illuminates New Dimensions of Amyloid Peptide-Membrane Interactions.Biophysical journal · 2020Article
- Impact of semen-derived amyloid (SEVI) on sperm viability and motility: its implication in male reproductive fitness.European biophysics journal : EBJ · 2019Article
- Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy.The Journal of biological chemistry · 2019Article
- 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
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of fibrillar aggregates has long been associated with neurodegenerative disorders such as Alzheimer and Parkinson diseases. Although fibrils are still considered important to the pathology of these disorders, it is now widely understood that smaller amyloid oligomers are the toxic entities along the misfolding pathway. One characteristic shared by the majority of amyloid oligomers is the ability to disrupt membranes, a commonality proposed to be responsible for their toxicity, although the mechanisms linking this to cell death are poorly understood. Here, we describe the physical basis for the cytotoxicity of oligomers formed by the prion protein (PrP)-derived amyloid peptide PrP(106-126). We show that oligomers of this peptide kill several mammalian cells lines, as well as mouse cerebellar organotypic cultures, and we also show that they exhibit antimicrobial activity. Physical perturbation of model membranes mimicking bacterial or mammalian cells was investigated using atomic force microscopy, polarized total internal reflection fluorescence microscopy, and NMR spectroscopy. Disruption of anionic membranes proceeds through a carpet or detergent model as proposed for other antimicrobial peptides. By contrast, when added to zwitterionic membranes containing cholesterol-rich ordered domains, PrP(106-126) oligomers induce a loss of domain separation and decreased membrane disorder. Loss of raft-like domains may lead to activation of apoptotic pathways, resulting in cell death. This work sheds new light on the physical mechanisms of amyloid cytotoxicity and is the first to clearly show membrane type-specific modes of action for a cytotoxic peptide.
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