ArticleBiochimica et biophysica acta. Proteins and proteomics2019
Assembly of α-synuclein aggregates on phospholipid bilayers.
Article in Biochimica et biophysica acta. Proteins and proteomics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 47 citations in OpenAlex.
- Large-scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation.FEBS open bio · 2026Article
- Uncovering Amyloid-β Interactions: Gray versus White Matter.ACS chemical neuroscience · 2025Article
- Martini 3 coarse-grained model of enzymes: Framework with validation by all-atom simulations and x-ray diffraction measurements.The Journal of chemical physics · 2025Article
- EnSCAN: ENsemble Scoring for prioritizing CAusative variaNts across multiplatform GWASs for late-onset alzheimer's disease.BioData mining · 2025Article
- High-resolution structural information of membrane-bound α-synuclein provides insight into the MoA of the anti-Parkinson drug UCB0599.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dark peptide discs for the investigation of membrane proteins in supported lipid bilayers: the case of synaptobrevin 2 (VAMP2).Nanoscale advances · 2022Article
- Free Cholesterol Accelerates Aβ Self-Assembly on Membranes at Physiological Concentration.International journal of molecular sciences · 2022Article
- Hybrid resolution molecular dynamics simulations of amyloid proteins interacting with membranes.Methods (San Diego, Calif.) · 2022Article
- An Update on the Critical Role of α-Synuclein in Parkinson's Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels.Molecular neurobiology · 2022Review
- Topographically smooth and stable supported lipid bilayer for high-resolution AFM studies.Methods (San Diego, Calif.) · 2022Article
- Phosphatidylserine, inflammation, and central nervous system diseases.Frontiers in aging neuroscience · 2022Review
- Review
- Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease.International journal of molecular sciences · 2020Review
- Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.Molecular neurodegeneration · 2020Article
- Differentiating Luminal and Membrane-Associated Nuclear Envelope Proteins.Biophysical journal · 2020Article
- Initiation and propagation of α-synuclein aggregation in the nervous system.Molecular neurodegeneration · 2020Review
- Interaction of Aβ42 with Membranes Triggers the Self-Assembly into Oligomers.International journal of molecular sciences · 2020Article
- Amyloid B-Protein Aggregation at Physiologically Relevant Concentrations. A Critical Role of Membranes.Alzheimer's research & therapy open access · 2020Article
- α-Synuclein-112 Impairs Synaptic Vesicle Recycling Consistent With Its Enhanced Membrane Binding Properties.Frontiers in cell and developmental biology · 2020Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The spontaneous self-assembly of α-synuclein (α-syn) into aggregates of different morphologies is associated with the development of Parkinson's disease. However, the mechanism behind the spontaneous assembly remains elusive. The current study shows a novel effect of phospholipid bilayers on the assembly of the α-syn aggregates. Using time-lapse atomic force microscopy, it was discovered that α-syn assembles into aggregates on bilayer surfaces, even at the nanomolar concentration range. The efficiency of the aggregation process depends on the membrane composition, with the greatest efficiency observed for of 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-l-serine (POPS). Importantly, assembled aggregates can dissociate from the surface, suggesting that on-surface aggregation is a mechanism by which pathological aggregates may be produced. Computational modeling revealed that dimers of α-syn assembled rapidly, through the membrane-bound monomer on POPS bilayer, due to an aggregation-prone orientation of α-syn. Interaction of α-syn with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) leads to a binding mode that does not induce a fast assembly of the dimer. Based on these findings, we propose a model in which the interaction of α-syn with membranes plays a critical role initiating the formation of α-syn aggregates and the overall aggregation process.
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