ArticleProceedings of the National Academy of Sciences of the United States of America2024
Toward the quantification of α-synuclein aggregates with digital seed amplification assays.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Profiling Protein Aggregate Size Using Single-Molecule Array Technology.Analytical chemistry · 2026Article
- A Systematic Comparison of Alpha-Synuclein Seed Amplification Assays for Increasing Reproducibility.Annals of clinical and translational neurology · 2026Review
- Digital seed amplification assay for TDP-43 aggregate quantification in CSF.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026Article
- Seed Amplification Assays for Parkinson's Disease: A Review of α-Synuclein Assays in Body Fluids and Tissues.Journal of neurochemistry · 2026Review
- The amplification of α-synuclein amyloid fibrils.Biochemical Society transactions · 2026Review
- Collaborative action for biomarker breakthroughs: Validating α-synuclein seed amplification assays in Parkinson's disease.Journal of Parkinson's disease · 2026Review
- When Proteins Go MAD-Misfolded, Amplified, Detected: Advances in α-Synuclein Pathophysiology and RT-QuIC Detection.Molecular neurobiology · 2026Review
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Ultrasonic frequency and intensity dependence in βUltrasonics sonochemistry · 2025Article
- Dermal Alpha-Synuclein Aggregation in Seed Amplification Assays for Parkinson's Disease Subtype Differentiation.European journal of neurology · 2025Article
- Digital seed amplification assay for TDP-43 aggregate quantification in CSF.medRxiv : the preprint server for health sciences · 2025Article
- Direct single-molecule detection and super-resolution imaging with a low-cost portable smartphone-based microscope.Nature communications · 2025Article
- Micro- and nanoscale biosensing technologies for early diagnosis of Parkinson's disease.Mikrochimica acta · 2025Review
- Ultrasonic detection of α-synuclein amyloid seeds from a highly crowded environment.Biophysical journal · 2025Article
- Seeding amplification assay: Limitations and insights for enhanced clinical and research applications.Journal of Parkinson's disease · 2025Review
- The Amplification of Alpha-Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions.Angewandte Chemie (International ed. in English) · 2025Article
- A same day α-synuclein RT-QuIC seed amplification assay for synucleinopathy biospecimens.Npj biosensing · 2025Article
- Biomarker-Based Approach to α-Synucleinopathies: Lessons from Neuropathology.Movement disorders : official journal of the Movement Disorder Society · 2024Article
- Intercellular transmission of alpha-synuclein.Frontiers in molecular neuroscience · 2024Review
- Studies on curcumin-glucoside in the prevention of alpha-synuclein aggregation.Journal of Alzheimer's disease reportsArticle
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Authors and funding
15 authors.
Funding
Abstract
The quantification and characterization of aggregated α-synuclein in clinical samples offer immense potential toward diagnosing, treating, and better understanding neurodegenerative synucleinopathies. Here, we developed digital seed amplification assays to detect single α-synuclein aggregates by partitioning the reaction into microcompartments. Using pre-formed α-synuclein fibrils as reaction seeds, we measured aggregate concentrations as low as 4 pg/mL. To improve our sensitivity, we captured aggregates on antibody-coated magnetic beads before running the amplification reaction. By first characterizing the pre-formed fibrils with transmission electron microscopy and size exclusion chromatography, we determined the specific aggregates targeted by each assay platform. Using brain tissue and cerebrospinal fluid samples collected from patients with Parkinson's Disease and multiple system atrophy, we demonstrated that the assay can detect endogenous pathological α-synuclein aggregates. Furthermore, as another application for these assays, we studied the inhibition of α-synuclein aggregation in the presence of small-molecule inhibitors and used a custom image analysis pipeline to quantify changes in aggregate growth and filament morphology.
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