ArticleBiophysical journal2009
The influence of vesicle size and composition on alpha-synuclein structure and stability.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 87 citations in OpenAlex.
- Synaptic vesicle architecture modulates α-synuclein conformation and pathogenic transitions in Parkinson's disease.Bioscience reports · 2026Review
- Cholesterol differentially regulates α-synuclein binding across membrane packing regimes.bioRxiv : the preprint server for biology · 2026Article
- Membrane Phase, Charge, and Curvature Regulate α-Synuclein Binding Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Exploring α-Syn's Functions Through Ablation Models: Physiological and Pathological Implications.Cellular and molecular neurobiology · 2025Review
- Cholesterol Accelerates Aggregation of α-Synuclein Simultaneously Increasing the Toxicity of Amyloid Fibrils.ACS chemical neuroscience · 2024Article
- Elucidation of molecular mechanisms by which amyloid βBiochimica et biophysica acta. Molecular and cell biology of lipids · 2024Article
- Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers.NPJ Parkinson's disease · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Article
- Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.Nature communications · 2023Article
- Protein kinase R dependent phosphorylation of α-synuclein regulates its membrane binding and aggregation.PNAS nexus · 2022Article
- Glycation modulates alpha-synuclein fibrillization kinetics: A sweet spot for inhibition.The Journal of biological chemistry · 2022Article
- A Triple Role for a Bilayer: Using Nanoliposomes to Cross and Protect Cellular Membranes.The Journal of membrane biology · 2021Article
- Lipid Metabolism Influence on Neurodegenerative Disease Progression: Is the Vehicle as Important as the Cargo?Frontiers in molecular neuroscience · 2021Review
- An intact membrane is essential for small extracellular vesicle-induced modulation of α-synuclein fibrillization.Journal of extracellular vesicles · 2020Article
- Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.Molecules (Basel, Switzerland) · 2020Review
- Unroofing site-specific α-synuclein-lipid interactions at the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The role of lipids in α-synuclein misfolding and neurotoxicity.The Journal of biological chemistry · 2019Review
- Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structures.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Oleuropein derivatives from olive fruit extracts reduce α-synuclein fibrillation and oligomer toxicity.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monomeric alpha-synuclein (alphaSN), which has no persistent structure in aqueous solution, is known to bind to anionic lipids with a resulting increase in alpha-helix structure. Here we show that at physiological pH and ionic strength, alphaSN incubated with different anionic lipid vesicles undergoes a marked increase in alpha-helical content at a temperature dictated either by the temperature of the lipid phase transition, or (in 1,2-DilauroylSN-Glycero-3-[Phospho-rac-(1-glycerol)] (DLPG), which is fluid down to 0 degrees C) by an intrinsic cold denaturation that occurs around 10-20 degrees C. This structure is subsequently lost in a thermal transition around 60 degrees C. Remarkably, this phenomenon is only observed for vesicles >100 nm in diameter and is sensitive to lipid chain length, longer chain lengths, and larger vesicles giving more cooperative unfolding transitions and a greater degree of structure. For both vesicle size and chain length, a higher degree of compressibility or permeability in the lipid thermal transition region is associated with a higher degree of alphaSN folding. Furthermore, the degree of structural change is strongly reduced by an increase in ionic strength or a decrease in the amount of anionic lipid. A simple binding-and-folding model that includes the lipid phase transition, exclusive binding of alphaSN to the liquid disordered phase, the thermodynamics of unfolding, and the electrostatics of binding of alphaSN to lipids is able to reproduce the two thermal transitions as well as the effect of ionic strength and anionic lipid. Thus the nature of alphaSN's binding to phospholipid membranes is intimately tied to the lipids' physico-chemical properties.
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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.