A photo of a microplate loaded onto the FLUOstar® Omega’s plate carrier.
The FLUOstar® Omega’s microplate carrier maintains plate stability throughout the many shaking cycles used in the real-time quaking-induced conversion assay.
BMG LABTECH

Scientists have associated many neurodegenerative disorders including Alzheimer’s, Parkinson’s, Huntington’s, and prion diseases with protein misfolding and aggregation, where incorrectly folded proteins act as seeds converting properly folded proteins into the disease form.1 This leads to insoluble protein aggregate formation. Previously, researchers inoculated animal models with samples derived from humans or animals with a suspected prion disease, such as Creutzfeldt-Jakob disease, bovine spongiform encephalopathy, or scrapie, to detect misfolded prion proteins and estimate their levels.2 However, these bioassays were time-intensive, taking several months to complete, and were expensive. 

To overcome these limitations, scientists developed the real-time quaking-induced conversion (RT-QuIC) assay for both research and diagnostic use, where prion seeds taken from specimens induce protein aggregation inside a microplate’s well.3 Because of intermittent shaking and the incubation temperature, scientists can complete RT-QuIC assays in as short as 20–60 hours, while maintaining or exceeding the sensitivity of animal-based approaches. Additionally, researchers have also adapted this bioassay to study protein aggregation in Alzheimer’s and Parkinson’s diseases.

The scientists that originally developed the RT-QuIC assay employed BMG LABTECH’s FLUOstar® Omega microplate reader due to its ability to withstand the harsh and prolonged shaking cycles required for this experiment, while periodically quantifying the samples. Using this instrument, researchers can perform the bioassays continuously over multiple days, increasing their throughput and efficiency. Thanks to its innovative capabilities, scientists worldwide continue to employ this microplate reader for prion detection and aggregation assays of other misfolded proteins with neurological relevance, such as α-synuclein, amyloid-β, and tau.

Learn more about this microplate reader’s advanced features. 


What methods do you use to measure protein aggregation?

Submit your Answer

  1. Yakubu UM, et al. Open Biol. 2020;10(11):200282.
  2. Wilham JM, et al. PLOS Pathog. 2010;6(12):e1001217.
  3. Manca M, Kraus A. Biomolecules. 2020;10(9):1233.
Learn More