ArticleScience advances2023
Two-color coincidence single-molecule pulldown for the specific detection of disease-associated protein aggregates.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Single-molecule validation and optimised protocols for the use of secondary nanobodies in multiplexed immunoassays.Journal of microscopy · 2026Article
- Fluorescence Characterization of Extracellular Vesicles Using Single-Molecule Confocal Microscopy.Small methods · 2025Article
- Sequential replacement of PSD95 subunits in postsynaptic supercomplexes is slowest in the cortex.eLife · 2024Article
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Authors and funding
19 authors.
Funding
Abstract
Protein misfolding and aggregation is a characteristic of many neurodegenerative disorders, including Alzheimer's and Parkinson's disease. The oligomers generated during aggregation are likely involved in disease pathogenesis and present promising biomarker candidates. However, owing to their small size and low concentration, specific tools to quantify and characterize aggregates in complex biological samples are still lacking. Here, we present single-molecule two-color aggregate pulldown (STAPull), which overcomes this challenge by probing immobilized proteins using orthogonally labeled detection antibodies. By analyzing colocalized signals, we can eliminate monomeric protein and specifically quantify aggregated proteins. Using the aggregation-prone alpha-synuclein protein as a model, we demonstrate that this approach can specifically detect aggregates with a limit of detection of 5 picomolar. Furthermore, we show that STAPull can be used in a range of samples, including human biofluids. STAPull is applicable to protein aggregates from a variety of disorders and will aid in the identification of biomarkers that are crucial in the effort to diagnose these diseases.
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