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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
Published on: November 20, 2018
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Study of Tau Liquid-Liquid Phase Separation In Vitro
Solomiia Boyko1, Witold K Surewicz2
1Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, USA.
Methods in Molecular Biology (Clifton, N.J.)
|October 31, 2022
Summary
Microtubule-associated protein tau aggregation drives neurodegenerative diseases. This study explores how liquid-liquid phase separation (LLPS) of tau protein in vitro may accelerate pathological aggregation, offering new research protocols.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Microtubule-associated protein tau aggregation is a hallmark of Alzheimer's disease and other neurodegenerative disorders.
- Recent studies indicate purified tau can undergo liquid-liquid phase separation (LLPS) in vitro, forming liquid droplets.
- Tau protein within these droplets shows accelerated transition to fibrillar aggregates, suggesting a role for LLPS in pathological tau aggregation.
Purpose of the Study:
- To investigate the role of liquid-liquid phase separation (LLPS) in the pathological aggregation of tau.
- To provide robust protocols for studying tau's LLPS behavior in vitro.
Main Methods:
- Turbidimetric assays to monitor aggregation.
- Light microscopy-based methods to visualize phase separation and droplet formation.
- Use of recombinant full-length tau protein.
Main Results:
- Demonstrated protocols for studying tau LLPS.
- Observed tau protein forming liquid droplets in vitro.
- Found accelerated fibrillar aggregation of tau within these liquid droplets.
Conclusions:
- Liquid-liquid phase separation (LLPS) is a potential mechanism contributing to tau pathology in neurodegenerative diseases.
- The described methods facilitate further research into tau aggregation and LLPS.
