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Related Experiment Video

Updated: Oct 26, 2025

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

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Hepta-Histidine Inhibits Tau Aggregation.

Kanoh Kondo1, Teikichi Ikura2, Hikari Tanaka1

  • 1Department of Neuropathology, Medical Research Institute and Center for Brain Integration Research, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan.

ACS Chemical Neuroscience
|July 28, 2021
PubMed
Summary

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Hepta-histidine (7H) inhibits Tau aggregation in vitro and reduces Tau phosphorylation in neurons. This peptide shows promise as a therapeutic for Tau-related neurodegenerative diseases like Alzheimer's disease.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Drug Discovery

Background:

  • Tau aggregation is a key feature of neurodegenerative diseases, including Alzheimer's disease (AD).
  • Targeting Tau aggregation is a significant strategy for therapeutic development in tauopathies.

Purpose of the Study:

  • To investigate the potential of hepta-histidine (7H) as an inhibitor of Tau aggregation.
  • To evaluate the efficacy of a cell-permeable TAT-7H conjugate in neuronal models of tauopathies.

Main Methods:

  • In vitro assays to assess the effect of 7H on Tau-R3 peptide aggregation.
  • Synthesis of a TAT-7H conjugate to enhance cellular uptake.
  • Treatment of induced pluripotent stem cell (iPSC)-derived neurons with TAT-7H to evaluate Tau phosphorylation.
Keywords:
Hepta-histidineTATaggregationneurodegenerative diseasestau

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Related Experiment Videos

Last Updated: Oct 26, 2025

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09:49

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

Published on: November 20, 2018

19.1K
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
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Main Results:

  • Hepta-histidine (7H) demonstrated suppression of Tau-R3 peptide aggregation in vitro.
  • The TAT-7H conjugate exhibited increased cell permeability.
  • TAT-7H treatment reduced Tau phosphorylation in iPSC-derived neurons with Tau or APP mutations.

Conclusions:

  • Hepta-histidine (7H) is a potential lead compound for developing anti-aggregation drugs.
  • TAT-7H represents a promising therapeutic strategy for Tau-related neurodegenerative diseases, including Alzheimer's disease.