Electric Double Layer Phenomena Near Surfaces Irreversibly Trigger Assembly of Tau Protein

. Assembly occurs on different electrode materials at identical effective electric fields, demonstrating independence from the electrode hydrophobicity and electronic structure. Surface-enhanced infrared absorption and plasmon resonance spectroscopies show that near-surface electric fields of ∼1 MV/cm trigger K18 folding and assembly. Ion ordering and charge screening near electrodes at higher salt concentrations (50 vs 1 mM) also reduce Coulombic repulsion between protein monomers and their cationic residues, promoting folding and assembly. Overall, these results show that interfacial electric fields and other non-Faradaic processes can reveal and drive protein misfolding and aggregation, hallmarks of tauopathies and prion-related neurodegenerative diseases.

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Publication Details

Journal
Journal of the American Chemical Society
Published
2026-04-01
DOI
https://doi.org/10.1021/jacs.5c23171
Primary Topic
Alzheimer's disease research and treatments
Type
article
Field-Weighted Citation Impact
0.00

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article

Electric Double Layer Phenomena Near Surfaces Irreversibly Trigger Assembly of Tau Protein

Norleakvisoth Lim, Eloïse Masquelier, Michael J. Gordon, Lior Sepunaru et al.
Journal of the American Chemical Society
Alzheimer's disease research and treatments
article

Electric Double Layer Phenomena Near Surfaces Irreversibly Trigger Assembly of Tau Protein

Norleakvisoth Lim, Eloïse Masquelier, Michael J. Gordon, Lior Sepunaru, Madeline H. Hicks, J. I. Yi, Daniel E. Morse
article en

Abstract

. Assembly occurs on different electrode materials at identical effective electric fields, demonstrating independence from the electrode hydrophobicity and electronic structure. Surface-enhanced infrared absorption and plasmon resonance spectroscopies show that near-surface electric fields of ∼1 MV/cm trigger K18 folding and assembly. Ion ordering and charge screening near electrodes at higher salt concentrations (50 vs 1 mM) also reduce Coulombic repulsion between protein monomers and their cationic residues, promoting folding and assembly. Overall, these results show that interfacial electric fields and other non-Faradaic processes can reveal and drive protein misfolding and aggregation, hallmarks of tauopathies and prion-related neurodegenerative diseases.

Journal of the American Chemical SocietyVol. 148(14)
California Institute of Technology (US), University of California System (US), Material (Belgium) (BE), Institut thématique Génétique, génomique et bioinformatique (FR), Institute for Collaborative Biotechnologies
Army Research Office, Institute for Collaborative Biotechnologies
Openalex Percentile: Top 27%
Alzheimer's disease research and treatments
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