ArticleScientific reports2016
Intrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanopores.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Solid-state nanopore sensing: the next workhorse of biophysical characterization.Nature methods · 2026Review
- Micro- and nanoscale biosensing technologies for early diagnosis of Parkinson's disease.Mikrochimica acta · 2025Review
- Carbon-based nanotechnology for Parkinson's disease: diagnostic and therapeutic innovations.Nanomedicine (London, England) · 2025Review
- Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025Review
- Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches.Small methods · 2024Review
- VAMP2 chaperones α-synuclein in synaptic vesicle co-condensates.Nature cell biology · 2024Article
- Multiplexed Digital Characterization of Misfolded Protein Oligomers via Solid-State Nanopores.Journal of the American Chemical Society · 2023Article
- Single-Molecule Detection of α-Synuclein Oligomers in Parkinson's Disease Patients Using Nanopores.ACS nano · 2023Article
- Molecular Sensing and Manipulation of Protein Oligomerization in Membrane Nanotubes with Bolaamphiphilic Foldamers.Journal of the American Chemical Society · 2023Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- Over One Million DNA and Protein Events Through Ultra-Stable Chemically-Tuned Solid-State Nanopores.Small (Weinheim an der Bergstrasse, Germany) · 2023Article
- Investigation of α-Synuclein and Amyloid-β(42)-E22Δ Oligomers Using SiN Nanopore Functionalized with L-Dopa.Chemistry, an Asian journal · 2022Article
- Localized Nanopore Fabrication via Controlled Breakdown.Nanomaterials (Basel, Switzerland) · 2022Review
- Nanopore sensors for viral particle quantification: current progress and future prospects.Bioengineered · 2021Review
- Lipid Species Dependent Vesicles Clustering Caused by alpha-Synuclein as Revealed by Single-Vesicle Imaging with Total Internal Reflection Fluorescence Microscopy.Biophysics reports · 2021Article
- Sensing with Nanopores and Aptamers: A Way Forward.Sensors (Basel, Switzerland) · 2020Review
- On-Chip Detection of the Biomarkers for Neurodegenerative Diseases: Technologies and Prospects.Micromachines · 2020Review
- Single-vesicle imaging quantifies calcium's regulation of nanoscale vesicle clustering mediated by α-synuclein.Microsystems & nanoengineering · 2020Article
- Single molecule sensing of amyloid-β aggregation by confined glass nanopores.Chemical science · 2019Article
- Single-vesicle measurement of protein-induced membrane tethering.Colloids and surfaces. B, Biointerfaces · 2019Article
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Authors and funding
10 authors.
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Abstract
α-Synuclein (α-Syn) is an abundant cytosolic protein involved in the release of neurotransmitters in presynaptic terminal and its aberrant aggregation is found to be associated with Parkinson's disease. Recent study suggests that the oligomers formed at the initial oligomerization stage may be the root cause of cytotoxicity. While characterizing this stage is challenging due to the inherent difficulties in studying heterogeneous and transient systems by conventional biochemical technology. Here we use solid-state nanopores to study the time-dependent kinetics of α-Syn oligomerization through a label-free and single molecule approach. A tween 20 coating method is developed to inhibit non-specific adsorption between α-Syn and nanopore surface to ensure successful and continuous detection of α-Syn translocation. We identify four types of oligomers formed in oligomerization stage and find an underlying consumption mechanism that the formation of large oligomers consumes small oligomers. Furthermore, the effect of lipid membrane on oligomerization of α-Syn is also investigated and the results show that 1,2-dioleoyl-sn-glycero-3-[phospho-L-serine] (DOPS) small unilamellar vesicles (SUVs) dramatically enhances the aggregation rate of α-Syn while do not alter the aggregation pathway.
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