ArticleProtein science : a publication of the Protein Society2011
Lipid composition influences the release of Alzheimer's amyloid β-peptide from membranes.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 87 citations in OpenAlex.
- Article
- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- The Influence of POPC as a Coaggregate in Amyloid-β Oligomer Formation.ACS chemical neuroscience · 2025Article
- Binding mechanism of full-length Aβ40 peptide to a mixed lipid bilayer.Frontiers in chemistry · 2024Article
- Lipidomics and proteomics: An integrative approach for early diagnosis of dementia and Alzheimer's disease.Frontiers in genetics · 2023Review
- Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane.Protein science : a publication of the Protein Society · 2022Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- The F19W mutation reduces the binding affinity of the transmembrane AβRSC advances · 2021Article
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- The S1P-S1PR Axis in Neurological Disorders-Insights into Current and Future Therapeutic Perspectives.Cells · 2020Review
- Lipid rafts and neurodegeneration: structural and functional roles in physiologic aging and neurodegenerative diseases.Journal of lipid research · 2020Review
- Computer simulations of protein-membrane systems.Progress in molecular biology and translational science · 2020Article
- Revealing a Dual Role of Ganglioside Lipids in the Aggregation of Membrane-Associated Islet Amyloid Polypeptide.The Journal of membrane biology · 2019Article
- Lipid and Lipid Raft Alteration in Aging and Neurodegenerative Diseases: A Window for the Development of New Biomarkers.International journal of molecular sciences · 2019Review
- Lipid Metabolism in Late-Onset Alzheimer's Disease Differs from Patients Presenting with Other Dementia Phenotypes.International journal of environmental research and public health · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- 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
- Cause and consequence of Aβ - Lipid interactions in Alzheimer disease pathogenesis.Biochimica et biophysica acta. Biomembranes · 2018Review
- The Effects of Extracellular Serum Concentration on APP Processing in Npc1-Deficient APP-Overexpressing N2a Cells.Molecular neurobiology · 2018Article
- Embedded in the Membrane: How Lipids Confer Activity and Specificity to Intramembrane Proteases.The Journal of membrane biology · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The behavior of the amyloid β-peptide (Aβ) within a membrane environment is integral to its toxicity and the progression of Alzheimer's disease. Ganglioside GM1 has been shown to enhance the aggregation of Aβ, but the underlying mechanism is unknown. Using atomistic molecular dynamics simulations, we explored the interactions between the 40-residue alloform of Aβ (Aβ(40) ) and several model membranes, including pure palmitoyloleoylphosphatidylcholine (POPC) and palmitoyloleoylphosphatidylserine (POPS), an equimolar mixture of POPC and palmitoyloleoylphosphatidylethanolamine (POPE), and lipid rafts, both with and without GM1, to understand the behavior of Aβ(40) in various membrane microenvironments. Aβ(40) remained inserted in POPC, POPS, POPC/POPE, and raft membranes, but in several instances exited the raft containing GM1. Aβ(40) interacted with GM1 largely through hydrogen bonding, producing configurations containing β-strands with C-termini that, in some cases, exited the membrane and became exposed to solvent. These observations provide insight into the release of Aβ from the membrane, a previously uncharacterized process of the Aβ aggregation pathway.
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