ArticleThe journal of physical chemistry letters2021
Structurally Distinct Polymorphs of Tau Aggregates Revealed by Nanoscale Infrared Spectroscopy.
Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Antiamyloid Antibody Effects on Aβ-42 Protein Aggregates Profiled Using Nanospectroscopy.Chemical & biomedical imaging · 2026Article
- Reversibility and β-sheet formation are decoupled in tau condensate aging.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- IR-AMES uncovers structure and composition of Alzheimer's tau oligomers.bioRxiv : the preprint server for biology · 2026Article
- Strain-Distinct α-Synuclein and Tau Cross-Seeding Uncovered by Correlative Approach with Optical Photothermal Infrared Sub-Micron Imaging.Journal of the American Chemical Society · 2025Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
- The role of phospholipid saturation and composition in α-synuclein aggregation and toxicity: A dual in vitro and in vivo approach.Protein science : a publication of the Protein Society · 2025Article
- Fourier transform infrared spectroscopy detects distinct TAR DNA-binding protein 43 signatures in frontotemporal lobar degeneration.Frontiers in neuroscience · 2025Article
- Structural diversity of Alzheimer-related protein aggregations revealed using photothermal ratio-metric micro-spectroscopy.Biomedical optics express · 2024Article
- Identification of tauopathy-associated lipid signatures in Alzheimer's disease mouse brain using label-free chemical imaging.Communications biology · 2024Article
- Under Heparin-Free Conditions Unsaturated Phospholipids Inhibit the Aggregation of 1N4R and 2N4R Tau.The journal of physical chemistry letters · 2024Article
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Structural characterization of amyloid aggregates with spatially resolved infrared spectroscopy.Methods in enzymology · 2024Article
- α-Synuclein emulsifies TDP-43 prion-like domain-RNA liquid droplets to promote heterotypic amyloid fibrils.Communications biology · 2023Article
- Intermediate Antiparallel Fibrils in Aβ40 Dutch Mutant Aggregation: Insights from Nanoscale Infrared Spectroscopy.The journal of physical chemistry. B · 2023Article
- Mid-infrared chemical imaging of intracellular tau fibrils using fluorescence-guided computational photothermal microscopy.Light, science & applications · 2023Article
- Lipids uniquely alter the secondary structure and toxicity of amyloid beta 1-42 aggregates.The FEBS journal · 2023Article
- Intermediate antiparallel fibrils in Aβ40 Dutch mutant aggregation: nanoscale insights from AFM-IR.bioRxiv : the preprint server for biology · 2023Article
- β-Carotene, a Potent Amyloid Aggregation Inhibitor, Promotes Disordered Aβ Fibrillar Structure.International journal of molecular sciences · 2023Article
- Nanoscale Infrared Spectroscopy Identifies Parallel to Antiparallel β-Sheet Transformation of Aβ Fibrils.The journal of physical chemistry letters · 2022Article
- Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2022Review
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Abstract
Aggregation of the tau protein plays a central role in several neurodegenerative diseases collectively known as tauopathies, including Alzheimer's and Parkinson's disease. Tau misfolds into fibrillar β sheet structures that constitute the paired helical filaments found in neurofibrillary tangles. It is known that there can be significant structural heterogeneities in tau aggregates associated with different diseases. However, while structures of mature fibrils have been studied, the structural distributions in early-stage tau aggregates is not well-understood. In the present study, we use atomic force microscopy-IR to investigate nanoscale spectra of individual tau fibrils at different stages of aggregation and demonstrate the presence of multiple fibrillar polymorphs that exhibit different secondary structures. We further show that mature fibrils contain significant amounts of antiparallel β sheets. Our results are the very first application of nanoscale infrared spectroscopy to tau aggregates and underscore the promise of spatially resolved infrared spectroscopy for investigating protein aggregation.
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