ArticleAngewandte Chemie (International ed. in English)2024
Structural Mapping of Protein Aggregates in Live Cells Modeling Huntington's Disease.
Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- FILM: mapping organellar metabolism by mid-infrared photothermal-modulated fluorescence.Nature methods · 2026Article
- Resolving protein condensates and aggregates in vivo by boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM).Communications chemistry · 2026Article
- FILM: Mapping organellar metabolism by mid-infrared photothermal modulated fluorescence.ArXiv · 2026Article
- Article
- Feeling the vibes: Vibrational spectroscopic imaging of biomolecular assemblies in their natural environment.Applied physics reviews · 2025Article
- Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.The journal of physical chemistry. B · 2025Review
- Lipid mediated formation of antiparallel aggregates in cerebral amyloid angiopathy.Acta neuropathologica · 2025Article
- Metasurface-enhanced biomedical spectroscopy.Nanophotonics (Berlin, Germany) · 2025Review
- Mid-infrared Photothermal Imaging: Instrument and Life Science Applications.Analytical chemistry · 2024Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
While protein aggregation is a hallmark of many neurodegenerative diseases, acquiring structural information on protein aggregates inside live cells remains challenging. Traditional microscopy does not provide structural information on protein systems. Routinely used fluorescent protein tags, such as Green Fluorescent Protein (GFP), might perturb native structures. Here, we report a counter-propagating mid-infrared photothermal imaging approach enabling mapping of secondary structure of protein aggregates in live cells modeling Huntington's disease. By comparing mid-infrared photothermal spectra of label-free and GFP-tagged huntingtin inclusions, we demonstrate that GFP fusions indeed perturb the secondary structure of aggregates. By implementing spectra with small spatial step for dissecting spectral features within sub-micrometer distances, we reveal that huntingtin inclusions partition into a β-sheet-rich core and a ɑ-helix-rich shell. We further demonstrate that this structural partition exists only in cells with the [RNQ
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Registered trials
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