ArticlePloS one2019
Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 35 citations in OpenAlex.
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Article
- Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomers.NPJ Parkinson's disease · 2024Article
- Artificial intelligence-coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases.Science advances · 2023Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- Monitoring α-synuclein aggregation.Neurobiology of disease · 2023Review
- Alpha-synuclein oligomers alter the spontaneous firing discharge of cultured midbrain neurons.Frontiers in cellular neuroscience · 2023Article
- Single-Particle Analysis of the Interaction Between Molecules and Protein Aggregated Species by Dual-Color Time-Resolved Fluorescence Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Amyloids on Membrane Interfaces: Implications for Neurodegeneration.The Journal of membrane biology · 2022Review
- Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease.Nature communications · 2022Article
- Article
- αS Oligomers Generated from Interactions with a Polyunsaturated Fatty Acid and a Dopamine Metabolite Differentially Interact with Aβ to Enhance Neurotoxicity.ACS chemical neuroscience · 2021Article
- NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases.Nature reviews. Chemistry · 2021Review
- In situ kinetic measurements of α-synuclein aggregation reveal large population of short-lived oligomers.PloS one · 2021Article
- Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.Nano letters · 2020Article
- A mechanistic hypothesis for the impairment of synaptic plasticity by soluble Aβ oligomers from Alzheimer's brain.Journal of neurochemistry · 2020Review
- Polymorphic α-Synuclein Strains Modified by Dopamine and Docosahexaenoic Acid Interact Differentially with Tau Protein.Molecular neurobiology · 2020Article
- Fatty Acid-Binding Protein 3 is Critical for α-Synuclein Uptake and MPPInternational journal of molecular sciences · 2019Article
- Probing the Origin of the Toxicity of Oligomeric Aggregates of α-Synuclein with Antibodies.ACS chemical biology · 2019Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Parkinson's Disease (PD) is a neurodegenerative disease for which there currently is no cure. Aggregation of the pre-synaptic protein α-synuclein (aSN) into oligomers (αSOs) is believed to play a key role in PD pathology, but little is known about αSO formation in vivo and how they induce neurodegeneration. Both the naturally occurring polyunsaturated fatty acid docosahexaenoic acid (DHA) and the lipid peroxidation product 4-hydroxynonenal (HNE), strongly upregulated during ROS conditions, stimulate the formation of αSOs, highlighting a potential role in PD. Yet, insight into αSOs structure and biological effects is still limited as most oligomer preparations studied to date are heterogeneous in composition. Here we have aggregated aSN in the presence of HNE and DHA and purified the αSOs using size exclusion chromatography. Both compounds stimulate formation of spherical αSOs containing anti-parallel β-sheet structure which have the same shape as unmodified αSOs though ca. 2-fold larger. Furthermore, the yield and stabilities of these oligomers are significantly higher than for unmodified aSN. Both modified and unmodified αSOs permeabilize synthetic vesicles, show high co-localisation with glutamatergic synapses and decrease Long Term Potentiation (LTP), in line with the reported synaptotoxic effects of αSOs. We conclude that DHA- and HNE-αSOs are convenient models for pathogenic disease-associated αSOs in PD.
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