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In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

The role of the lipid bilayer in tau aggregation

Shana Elbaum-Garfinkle1, Trudy Ramlall, Elizabeth Rhoades

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, USA.

Biophysical Journal
|June 2, 2010
PubMed

Insights

Anionic lipid vesicles induce tau protein aggregation, a key factor in neurodegenerative diseases. This aggregation is triggered by exceeding a critical surface density of tau on the lipid bilayer.

Area of Science:

  • Biochemistry
  • Neuroscience
  • Cell Biology

Background:

  • Tau protein aggregation is a hallmark of neurodegenerative diseases.
  • Understanding the mechanisms driving tau aggregation is crucial for disease pathology insights.

Purpose of the Study:

  • To investigate how anionic lipid vesicles induce tau aggregation in vitro.
  • To elucidate the role of lipid bilayers in modulating tau protein interactions.

Main Methods:

  • Utilized K18, a tau fragment, and anionic lipid vesicles for in vitro aggregation studies.
  • Analyzed protein-lipid interactions, binding affinity, and aggregate formation using biophysical techniques.
  • Assessed aggregate characteristics using Thioflavin T binding assays.

Main Results:

  • Tau aggregation initiated when K18 bound to lipid bilayers exceeded a critical surface density.
  • Protein-lipid ratio at aggregation threshold and binding affinity were pH-dependent.
  • Aggregates comprised both protein and vesicles, exhibiting pathological characteristics via Thioflavin T binding.

Conclusions:

  • Lipid bilayers facilitate tau aggregation by screening protein charges and increasing local protein concentration.
  • Abundant anionic lipids in cellular membranes suggest a significant role in tau-lipid interactions relevant to disease.
  • Findings contribute to understanding the molecular mechanisms underlying tauopathies.

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