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<p>The interaction between cationic gold nanorods (GNRs) and tau protein was investigated to assess their potential in modulating tau aggregation, a central process in neurodegenerative diseases. Monodisperse GNRs with rod-shaped morphology (55 ± 4 nm length, 20 ± 3 nm width, aspect ratio ~2.75) and a defined longitudinal LSPR peak at 654 nm (FWHM ~77 nm) were synthesized. Incubation with tau (0–40 µM) caused only a slight decrease in LSPR intensity without peak shifts, confirming nanorod stability. Thioflavin T assays demonstrated potent, concentration-dependent inhibition of heparin-induced tau fibrillation, with ~70%, ~85%, and ~95% reduction in final ThT fluorescence at 5, 10, and 20 nM GNRs, respectively. Crucially, structural analyses via FT-IR and CD showed no significant transition to β-sheet content, preserving tau’s intrinsically disordered conformation. Fluorescence quenching studies revealed strong static quenching (K<sub>SV</sub> = 5.4 µM⁻<sup>1</sup>), indicating close proximity of tyrosine residues to the GNR surface likely through π–π stacking and hydrophobic interactions. This in vitro study establishes GNRs as effective, structure-preserving nanoscaffolds that inhibit tau aggregation by sequestering monomers. The key innovations of this work are the demonstration of this dual functionality, potent inhibition coupled with conformational preservation, and the elucidation of the anisotropic geometry of GNRs as a critical design parameter for achieving this structure-preserving mechanism. While promising, the mechanistic insights are limited to in vitro conditions, and further in vivo validation will be required.</p> Graphical Abstract <p></p>

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Gold nanorods as structure-preserving inhibitors of tau aggregation: biophysical and mechanistic insights

  • 期刊论文

  • 发表日期：

    2026年2月3日

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  • Hanna Ashrafpour,
  • Shahnaz Ashrafpour,
  • Reza Khodarahmi,
  • Soheila Mohammadi

摘要

The interaction between cationic gold nanorods (GNRs) and tau protein was investigated to assess their potential in modulating tau aggregation, a central process in neurodegenerative diseases. Monodisperse GNRs with rod-shaped morphology (55 ± 4 nm length, 20 ± 3 nm width, aspect ratio ~2.75) and a defined longitudinal LSPR peak at 654 nm (FWHM ~77 nm) were synthesized. Incubation with tau (0–40 µM) caused only a slight decrease in LSPR intensity without peak shifts, confirming nanorod stability. Thioflavin T assays demonstrated potent, concentration-dependent inhibition of heparin-induced tau fibrillation, with ~70%, ~85%, and ~95% reduction in final ThT fluorescence at 5, 10, and 20 nM GNRs, respectively. Crucially, structural analyses via FT-IR and CD showed no significant transition to β-sheet content, preserving tau’s intrinsically disordered conformation. Fluorescence quenching studies revealed strong static quenching (KSV = 5.4 µM⁻1), indicating close proximity of tyrosine residues to the GNR surface likely through π–π stacking and hydrophobic interactions. This in vitro study establishes GNRs as effective, structure-preserving nanoscaffolds that inhibit tau aggregation by sequestering monomers. The key innovations of this work are the demonstration of this dual functionality, potent inhibition coupled with conformational preservation, and the elucidation of the anisotropic geometry of GNRs as a critical design parameter for achieving this structure-preserving mechanism. While promising, the mechanistic insights are limited to in vitro conditions, and further in vivo validation will be required.

Graphical Abstract