ArticleNano letters2020
Rapid Structural, Kinetic, and Immunochemical Analysis of Alpha-Synuclein Oligomers in Solution.
Article in Nano letters, 2020. 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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Who cites it
20 citing papers in PubMed.
- Narrative Review "Dual Frontiers in Neurodegeneration: Pharmacological Synergies and Divergences in Parkinson's Disease and Type 2 Diabetes Mellitus".Cellular and molecular neurobiology · 2026Review
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Microfluidics for protein interaction studies: current methods, challenges, and future perspectives.European biophysics journal : EBJ · 2025Review
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
- Single-molecule digital sizing of proteins in solution.Nature communications · 2024Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Article
- A Potent Sybody Selectively Inhibits α-Synuclein Amyloid Formation by Binding to the P1 Region.Journal of medicinal chemistry · 2024Article
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.ACS chemical neuroscience · 2024Article
- Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning.Nature chemical biology · 2024Article
- Nonspecificity fingerprints for clinical-stage antibodies in solution.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores.Journal of the American Chemical Society · 2023Article
- α-Synuclein Aggregation Is Triggered by Oligomeric Amyloid-β 42 via Heterogeneous Primary Nucleation.Journal of the American Chemical Society · 2023Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- Galectin-3 shapes toxic alpha-synuclein strains in Parkinson's disease.Acta neuropathologica · 2023Article
- Single-Molecule Sizing through Nanocavity Confinement.Nano letters · 2023Article
- A Facile Method to Produce N-Terminally Truncated α-Synuclein.Frontiers in neuroscience · 2022Article
- Engineering of a protein probe with multiple inputs and multiple outputs for evaluation of alpha synuclein aggregation states.Biochemical engineering journal · 2022Article
- The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends.Nature communications · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Oligomers comprised of misfolded proteins are implicated as neurotoxins in the pathogenesis of protein misfolding conditions such as Parkinson's and Alzheimer's diseases. Structural, biophysical, and biochemical characterization of these nanoscale protein assemblies is key to understanding their pathology and the design of therapeutic interventions, yet it is challenging due to their heterogeneous, transient nature and low relative abundance in complex mixtures. Here, we demonstrate separation of heterogeneous populations of oligomeric α-synuclein, a protein central to the pathology of Parkinson's disease, in solution using microfluidic free-flow electrophoresis. We characterize nanoscale structural heterogeneity of transient oligomers on a time scale of seconds, at least 2 orders of magnitude faster than conventional techniques. Furthermore, we utilize our platform to analyze oligomer ζ-potential and probe the immunochemistry of wild-type α-synuclein oligomers. Our findings contribute to an improved characterization of α-synuclein oligomers and demonstrate the application of microchip electrophoresis for the free-solution analysis of biological nanoparticle analytes.
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