ArticleBiophysical journal2016
Membrane-Bound Alpha Synuclein Clusters Induce Impaired Lipid Diffusion and Increased Lipid Packing.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Familial mutations modulate α-synuclein interactions with key neuronal membrane lipids.The FEBS journal · 2026Article
- The role of phospholipid saturation and composition in α-synuclein aggregation and toxicity: A dual in vitro and in vivo approach.Protein science : a publication of the Protein Society · 2025Article
- MJF-14 proximity ligation assay detects early non-inclusion alpha-synuclein pathology with enhanced specificity and sensitivity.NPJ Parkinson's disease · 2024Article
- Elucidating the mechanisms of α-Synuclein-lipid interactions using site-directed mutagenesis.Neurobiology of disease · 2024Article
- Elucidation of molecular mechanisms by which amyloid βBiochimica et biophysica acta. Molecular and cell biology of lipids · 2024Article
- Length and saturation of choline plasmalogens alter the aggregation rate of α-synuclein but not the toxicity of amyloid fibrils.International journal of biological macromolecules · 2024Article
- Large Unilamellar Vesicles of Phosphatidic Acid Reduce the Toxicity of α-Synuclein Fibrils.Molecular pharmaceutics · 2024Article
- The influence of zwitterionic and anionic phospholipids on protein aggregation.Biophysical chemistry · 2024Review
- Alpha-Synuclein and Cognitive Decline in Parkinson Disease.Life (Basel, Switzerland) · 2021Review
- Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Membrane interactions of intrinsically disordered proteins: The example of alpha-synuclein.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- [The preparation of supported lipid bilayers and its functional study].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2019Article
- Folding and Lipid Composition Determine Membrane Interaction of the Disordered Protein COR15A.Biophysical journal · 2018Article
- Structural characteristics and membrane interactions of tandem α-synuclein oligomers.Scientific reports · 2018Article
- Quantitative mass imaging of single biological macromolecules.Science (New York, N.Y.) · 2018Article
- Critical appraisal of pathology transmission in the α-synuclein fibril model of Lewy body disorders.Experimental neurology · 2018Article
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- Effects of soft interactions and bound mobility on diffusion in crowded environments: a model of sticky and slippery obstacles.Physical biology · 2017Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aggregation of membrane-bound α-synuclein (αS) into oligomers and/or amyloid fibrils has been suggested to cause membrane damage in in vitro model phospholipid membrane systems and in vivo. In this study, we investigate how αS interactions that precede the formation of well-defined aggregates influence physical membrane properties. Using three truncated variants of αS with different aggregation propensities and comparable phospholipid membrane binding affinities we show, using fluorescence recovery after photobleaching (FRAP) and fluorescence anisotropy measurements, that formation of αS clusters on supported lipid bilayers (SLBs) impairs lateral lipid diffusion and increases lipid packing beneath the αS clusters. Formation of protein clusters starts immediately after monomer addition. The magnitudes of the changes in effective lipid diffusion and lipid order increase with the protein cluster size. Our results show that the combination of inter-αS and αS-membrane interactions can drive the formation of more ordered lipid domains. Considering the functional involvement of membrane micro-domains in biological membranes, αS-induced domain formation may be relevant for alternative disease mechanisms.
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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.