Chemical Imaging of RNA‐Tau Amyloid Fibrils at the Nanoscale Using Tip‐Enhanced Raman Spectroscopy

Author:

Cooney Gary Sean1,Talaga David1,Ury‐Thiery Vicky2,Fichou Yann2,Huang Yuhan1,Lecomte Sophie2,Bonhommeau Sébastien1ORCID

Affiliation:

1. University of Bordeaux CNRS Bordeaux INP, ISM, UMR 5255 33400 Talence France

2. University of Bordeaux CNRS Bordeaux INP, CBMN, UMR 5248 33600 Pessac France

Abstract

AbstractIn the presence of cofactors, tau protein can form amyloid deposits in the brain which are implicated in many neurodegenerative disorders. Heparin, lipids, and RNA are used to recreate tau aggregates in vitro from recombinant protein. However, the mechanism of interaction of these cofactors and the interactions between cofactors and tau are poorly understood. Herein, we use tip‐enhanced Raman spectroscopy (TERS) to visualize the spatial distribution of adenine, protein secondary structure, and amino acids (arginine, lysine and histidine) in single polyadenosine (polyA)‐induced tau fibrils with nanoscale spatial resolution (<10–20 nm). Based on reference unenhanced and surface‐enhanced Raman spectra, we show that the polyA anionic cofactor is incorporated in the fibril structure and seems to be superficial to the β‐sheet core, but nonetheless enveloped within the random‐coiled fuzzy coat. TERS images also prove the colocalization of positively charged arginine, lysine, and histidine amino acids and negatively charged polyA, which constitutes an important step forward to better comprehend the action of RNA cofactors in the mechanism of formation of toxic tau fibrils. TERS appears as a powerful technique for the identification of cofactors in individual tau fibrils and their mode of interaction.

Funder

Agence Nationale de la Recherche

Conseil Régional Aquitaine

HORIZON EUROPE European Research Council

Publisher

Wiley

Subject

General Chemistry,Catalysis

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