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Related Experiment Video

Updated: Dec 31, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Tau-Cofactor Complexes as Building Blocks of Tau Fibrils.

Yann Fichou¹, Zachary R Oberholtzer¹, Hoang Ngo¹

¹Department of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, CA, United States.

Frontiers in Neuroscience

|January 11, 2020

Summary

Cofactors are essential for inducing tau protein aggregation into fibrils, a key process in tauopathies. Understanding these interactions is crucial for developing therapeutic strategies against neurodegenerative diseases.

Keywords:

aggregation seeding cofactors conformational transformation protein aggregation tau oligomers tau protein tauopathies

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Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Tau protein aggregation into neurofibrillary tangles is a hallmark of tauopathies.
The precise mechanisms initiating and propagating tau aggregation remain unclear, even in vitro.
Polyanionic cofactors are commonly used to induce in vitro tau fibrillization.

Purpose of the Study:

To mechanistically investigate how cofactors induce tau fibrillization using biophysical characterizations.
To elucidate the role of cofactors in the conformational changes of tau protein.
To understand the regulation of tau aggregation by tau-cofactor interactions.

Main Methods:

In vitro aggregation assays of recombinant human tau protein.
Biophysical characterizations to study tau-cofactor interactions and complex formation.
Assessment of Thioflavin T (ThT) fluorescence to detect fibril formation.

Main Results:

Cofactors are the limiting factor for generating Thioflavin T-active tau fibrils and act as templating reactants.
Heparin demonstrates superior potency in recruiting monomeric tau compared to seeds.
Tau-cofactor complexes form, and their progression to fibrils is regulated by cofactor interactions.
Mild cofactors can form inert tau complexes, requiring a seed to overcome the energy barrier for fibrillization.

Conclusions:

Cofactors play a critical role in initiating tau aggregation by templating conformational changes.
The interaction between tau and cofactors is tightly regulated, influencing the formation of aggregation-competent species.
In cells, tau-cofactor complexes may exist in a metastable state, becoming irreversibly aggregated upon encountering a seed.