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

In 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...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2023-12, Vol.62 (50), p.e202314369-n/a
Main Authors: Cooney, Gary Sean, Talaga, David, Ury‐Thiery, Vicky, Fichou, Yann, Huang, Yuhan, Lecomte, Sophie, Bonhommeau, Sébastien
Format: Article
Language:English
Subjects:
Adenine
Amino Acids
Amyloid
Amyloid - chemistry
Arginine
Biochemistry, Molecular Biology
Biophysics
Cofactors
Fibrillogenesis
Heparin
Histidine
Life Sciences
Lipids
Lysine
Neurodegenerative diseases
Neuroimaging
Protein structure
Proteins
Raman spectra
Raman spectroscopy
Ribonucleic acid
RNA
Secondary structure
Spatial discrimination
Spatial distribution
Spatial resolution
Spectroscopy
Spectrum analysis
Spectrum Analysis, Raman - methods
Surface-Enhanced Raman Spectroscopy
Tau Protein
tau Proteins - metabolism
Tip-Enhanced Raman Spectroscopy
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Summary:In 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 (
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.202314369