ArticleThe Journal of biological chemistry2016
Distinct Membrane Disruption Pathways Are Induced by 40-Residue β-Amyloid Peptides.
Article in The Journal of biological chemistry, 2016. 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, 58 citations in OpenAlex.
- Structural convergence and membrane interactions of AβCommunications chemistry · 2025Article
- Modulation of Lipid Dynamics in the β-Amyloid Aggregates Induced Membrane Fragmentation.The journal of physical chemistry. B · 2024Article
- In-cellBiophysical chemistry · 2023Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- Ganglioside-Enriched Phospholipid Vesicles Induce Cooperative Aβ Oligomerization and Membrane Disruption.Biochemistry · 2022Article
- Membrane interaction to intercellular spread of pathology in Alzheimer's disease.Frontiers in neuroscience · 2022Review
- Structural differences in amyloid-β fibrils from brains of nondemented elderly individuals and Alzheimer's disease patients.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Amyloid-beta peptide (25-35) triggers a reorganization of lipid membranes driven by temperature changes.Scientific reports · 2021Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Application of DNP-enhanced solid-state NMR to studies of amyloid-β peptide interaction with lipid membranes.Chemistry and physics of lipids · 2021Article
- Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162.ACS chemical neuroscience · 2021Article
- Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.ACS chemical neuroscience · 2020Article
- Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β-Amyloid Oligomers.The journal of physical chemistry letters · 2020Article
- High-Throughput Screening at the Membrane Interface Reveals Inhibitors of Amyloid-β.Biochemistry · 2020Article
- Fibrillization of 40-Residue β-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms.Biomolecules · 2020Article
- Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.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
- Depletion of amyloid-β peptides from solution by sequestration within fibril-seeded hydrogels.Protein science : a publication of the Protein Society · 2018Article
- Lipid accelerating the fibril of islet amyloid polypeptide aggravated the pancreatic islet injury in vitro and in vivo.Lipids in health and disease · 2018Article
- Model Phospholipid Liposomes to Study the β-Amyloid-Peptide-Induced Membrane Disruption.Methods in molecular biology (Clifton, N.J.) · 2018Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellular membrane disruption induced by β-amyloid (Aβ) peptides has been considered one of the major pathological mechanisms for Alzheimer disease. Mechanistic studies of the membrane disruption process at a high-resolution level, on the other hand, are hindered by the co-existence of multiple possible pathways, even in simplified model systems such as the phospholipid liposome. Therefore, separation of these pathways is crucial to achieve an in-depth understanding of the Aβ-induced membrane disruption process. This study, which utilized a combination of multiple biophysical techniques, shows that the peptide-to-lipid (P:L) molar ratio is an important factor that regulates the selection of dominant membrane disruption pathways in the presence of 40-residue Aβ peptides in liposomes. Three distinct pathways (fibrillation with membrane content leakage, vesicle fusion, and lipid uptake through a temporarily stable ionic channel) become dominant in model liposome systems under specific conditions. These individual systems are characterized by both the initial states of Aβ peptides and the P:L molar ratio. Our results demonstrated the possibility to generate simplified Aβ-membrane model systems with a homogeneous membrane disruption pathway, which will benefit high-resolution mechanistic studies in the future. Fundamentally, the possibility of pathway selection controlled by P:L suggests that the driving forces for Aβ aggregation and Aβ-membrane interactions may be similar at the molecular level.
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