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

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

Published on: November 20, 2018

Structural determinants of Tau aggregation inhibitor potency.

Kelsey N Schafer¹, Katryna Cisek¹, Carol J Huseby¹

¹From the Department of Molecular and Cellular Biochemistry, College of Medicine, The Ohio State University, Columbus, Ohio 43210.

The Journal of Biological Chemistry

|September 28, 2013

Summary

Ligand polarizability, a measure of electron delocalization, directly correlates with the potency of small-molecule Tau aggregation inhibitors. These inhibitors stabilize soluble Tau oligomers, suggesting a new therapeutic strategy for Alzheimer disease.

Keywords:

Aggregation Alzheimer Disease Chemical biology Protein Structure Tau

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Area of Science:

Neuroscience
Biochemistry
Medicinal Chemistry

Background:

Small-molecule inhibitors of Tau aggregation are investigated for Alzheimer disease therapy.
Key features driving inhibitor potency and their molecular targets remain largely unidentified.

Purpose of the Study:

To test the hypothesis that ligand polarizability predicts Tau aggregation inhibitor potency.
To identify the molecular targets of these inhibitors within the Tau aggregation pathway.

Main Methods:

Ab initio quantum methods calculated ground state polarizabilities for cyanine, phenothiazine, and arylmethine derivatives.
Inhibitory potency was determined using octadecyl sulfate (SDS) inducer under reducing conditions.
Tau deletion and missense mutants were used to localize inhibitor binding sites.

Main Results:

Polarizability directly correlated with inhibitory potency across four inhibitor series.
Inhibitors stabilized soluble, SDS-resistant Tau species, reducing filamentous aggregates.
Cyanine binding was localized to the Tau microtubule-binding repeat region.
Inhibitor interaction occurred prior to Tau nucleus formation, dependent on SDS inducer.

Conclusions:

Flat, highly polarizable ligands inhibit Tau aggregation by targeting folded Tau species.
These ligands promote the formation of stable, soluble Tau oligomers, offering a potential therapeutic mechanism for Alzheimer disease.