Tau is a metal binding protein: Structural insights into copper and zinc coordination sites and their impact on amyloid aggregation.

Gerardo U. Juarez-Romero; Xun Sun; Juan Gerez; Christophe den Auwer; Gautier Landrot; Maarten Nachtegaal; Roland Riek; Jinghui Luo; Liliana Quintanar

doi:10.1039/d5sc08604c

January 1, 2026Chemical ScienceOpen Access

Tau is a metal binding protein: Structural insights into copper and zinc coordination sites and their impact on amyloid aggregation.

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Key Points

To explore how tau protein interacts with copper and zinc, and the implications for amyloid aggregation in Alzheimer's disease.
Structural analysis of tau protein to identify metal binding sites.
Assessment of copper and zinc coordination in tau protein.
Evaluation of amyloid aggregation in the presence of metal ions.
Identification of specific binding sites for copper and zinc on tau protein.
Demonstrated impact of metal ions on the aggregation behavior of amyloid proteins.
Findings suggest that disrupted metal ion homeostasis may contribute to tauopathy progression.

Implication

Investigates metal binding of tau protein and its effects on amyloid aggregation in Alzheimer's disease, suggesting significant implications for disease mechanisms.

Abstract

Tau protein is a microtubule-associated protein central to the pathogenesis of Alzheimer’s disease (AD) and other tauopathies. While metal ion homeostasis is disrupted in AD, the presence of copper and...

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Cite This Study

Juarez-Romero et al. (2026) studied this question.

synapsesocial.com/papers/698d6d795be6419ac0d526a1 https://doi.org/10.1039/d5sc08604c

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Tau is a metal binding protein: Structural insights into copper and zinc coordination sites and their impact on amyloid aggregation.

Key Points

Implication

Abstract

Discussion

Cite This Study

Tau is a metal binding protein: Structural insights into copper and zinc coordination sites and their impact on amyloid aggregation.

Key Points

Implication

Abstract

Discussion

Cite This Study

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