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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
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Effect of altered solution conditions on tau conformational dynamics: Plausible implication on order propensity and
Benita Jebarupa1, Monita Muralidharan1, Bindu Y Srinivasu1
1Clinical Proteomics Unit, Division of Molecular Medicine, St. John's Research Institute, St. John's National Academy of Health Sciences, 100 Feet Road, Koramangala, Bangalore 560034, Karnataka, India.
Biochimica Et Biophysica Acta. Proteins and Proteomics
|April 10, 2018
Summary
The study reveals how solution conditions like ionic strength affect tau protein structure. Altered tau conformation, influenced by these factors, may impact its role in neuronal function and disease.
Area of Science:
- Biochemistry
- Neuroscience
- Structural Biology
Background:
- Intrinsically disordered protein tau stabilizes microtubules in neurons.
- Tau's random coil structure is thought to be stable, but transient structures exist.
- Misfolded tau forms filaments in Alzheimer's disease, highlighting conformational importance.
Purpose of the Study:
- To investigate the impact of ionic strength, temperature, and solvent polarity on tau40 conformation.
- To understand how solution conditions influence tau's structural dynamics.
- To explore the link between tau conformation and its role in neuronal physiology and disease.
Main Methods:
- Ion mobility mass spectrometry was used to analyze tau40 conformational preferences.
- Collision cross-section measurements provided insights into molecular size changes.
- Limited proteolysis identified regions with varying order propensity.
Main Results:
- Low ionic strength, high temperature, and low solvent polarity induced tau40 collapse.
- High ionic strength caused tau40 expansion.
- Specific regions (projection domain, proline-rich, C-terminal) showed altered order propensity.
- Conformational changes did not increase heparin-induced aggregation but correlated with fibrillation propensity.
Conclusions:
- Solution conditions significantly alter tau40 conformation, affecting its structural dynamics.
- Regions prone to disorder-to-order transitions may influence microtubule interaction and signaling.
- Electrostatic interactions correlate with tau fibrillation, suggesting a link to disease-related hyperphosphorylation and self-assembly.
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