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Updated: May 9, 2026

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

Probing copper/tau protein interactions electrochemically.

Sanela Martic1, Meghan K Rains, Heinz-Bernhard Kraatz

  • 1Department of Chemistry, Oakland University, Rochester, NY 48309, USA.

Analytical Biochemistry
|August 3, 2013
PubMed
Summary
This summary is machine-generated.

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Copper(II) ions interact with tau protein, a key factor in Alzheimer's disease. This study used electrochemistry to show phosphorylated tau binds more copper than normal tau, suggesting a role in disease progression.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Electrochemistry

Background:

  • Alzheimer's disease (AD) involves protein misfolding and aggregation, influenced by metal ions like copper(II) [Cu(II)].
  • While copper(II) toxicity is studied in amyloid-beta (Aβ), its role in tau protein pathology is less understood.
  • Tau protein normally stabilizes microtubules, but hyperphosphorylation and aggregation in AD compromise its function.

Purpose of the Study:

  • To investigate the interaction between full-length tau-410 and copper(II) ions using an electrochemical approach.
  • To determine the influence of tau phosphorylation and pH on copper(II) binding.
  • To explore competitive metal ion binding effects, specifically zinc(II) [Zn(II)], on copper(II) coordination to tau.

Main Methods:

  • Electrochemical study of full-length tau-410 immobilized on gold surfaces.
Keywords:
BioelectrochemistryCopperElectrochemistryProteinTau

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  • Measurement of redox potentials and current intensities for Cu(II)-tau complexes at varying pH.
  • X-ray photoelectron spectroscopy (XPS) to confirm metal ion coordination.
  • Competitive binding assays with zinc(II) ions.

    • Main Results:

    • Copper(II) coordination to tau immobilized on gold surfaces generated a distinct electrochemical signal (approx. 140±5mV vs. Ag/AgCl).
    • Phosphorylated tau (pTau) films exhibited greater Cu(II) uptake compared to nonphosphorylated tau (nTau) films, particularly at lower pH.
    • Zinc(II) ions were found to displace Cu(II) from pTau films, indicating competitive binding.

    Conclusions:

    • Copper(II) ions play a significant role in tau biochemistry, with implications for Alzheimer's disease pathogenesis.
    • The differential binding of Cu(II) to pTau suggests a mechanism contributing to tau pathology and neurodegeneration.
    • Electrochemical techniques offer a sensitive method for studying metalloprotein interactions with minimal sample requirements.