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Related Experiment Video

Updated: Oct 10, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Three-repeat and four-repeat tau isoforms form different oligomers.

Hedieh Shahpasand-Kroner¹, Jennifer Portillo¹, Carter Lantz²

¹Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, California, USA.

Protein Science : a Publication of the Protein Society

|December 13, 2021

Summary

This summary is machine-generated.

Three-repeat (3R) tau isoforms form oligomers more readily than four-repeat (4R) tau isoforms. Current tau aggregation inhibitors do not affect this initial oligomerization process, suggesting 3R-tau oligomers as a novel therapeutic target.

Keywords:

inhibitor oligomerization tau isoforms tauopathies

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Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Tauopathies involve brain aggregates with specific tau isoforms and distinct tau strains.
Tau oligomers are neurotoxic, but their formation is poorly understood due to their metastable nature.
The influence of human tau isoform primary structures on oligomerization remains largely uncharacterized.

Purpose of the Study:

To investigate how the primary structures of the six human tau isoforms influence tau oligomer formation.
To assess the effect of known tau aggregation inhibitors on initial tau oligomerization.
To identify potential therapeutic targets for tauopathies.

Main Methods:

Analysis of initial tau oligomers using dot blots, native-PAGE/western blots, and mass spectrometry.
Utilized photo-induced cross-linking of unmodified proteins and ion-mobility spectroscopy.
Tested three classes of tau aggregation inhibitors: Methylene Blue, CLR01, and TLKIVW.

Main Results:

Three-repeat (3R) tau isoforms demonstrated a higher propensity for oligomer formation compared to four-repeat (4R) isoforms.
The tested tau aggregation inhibitors showed minimal to no effect on the initial oligomerization process.
This contrasts with their known inhibitory effects on tau fibrillation.

Conclusions:

The primary structure of tau isoforms significantly impacts their oligomerization behavior.
Initial tau oligomerization is distinct from tau fibrillation and may not be inhibited by current aggregation inhibitors.
Targeting 3R-tau oligomers presents a promising avenue for developing novel therapeutics for tauopathies.