ArticleThe journal of physical chemistry letters2021
Two-Photon Excited Polarization-Dependent Autofluorescence of Amyloids as a Label-Free Method of Fibril Organization Imaging.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- The influence of H-bonding network disruption on morphology, structure and autofluorescence of amyloids.Materials advances · 2026Article
- The carbonyl-lock mechanism underlying non-aromatic fluorescence in biological matter.Nature communications · 2023Article
- A Comprehensive Analysis of the Intrinsic Visible Fluorescence Emitted by Peptide/Protein Amyloid-like Assemblies.International journal of molecular sciences · 2023Review
- Article
- Label-free optical metabolic imaging of adipose tissues for prediabetes diagnosis.Theranostics · 2023Article
- One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids.The journal of physical chemistry letters · 2022Article
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5 authors.
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Abstract
Amyloids are broadly investigated protein misfolding products with characteristic β-sheet assemblies that have an important role in neurodegenerative diseases (e.g., Alzheimer's disease). While they are usually visualized by staining with Thioflavin-T, Congo Red, or other fluorescent markers, it still arouses a controversy over possible staining molecule influence on the amyloid structure or aggregation process. In this work we present, for the first time, the polarization analysis of two-photon excited autofluorescence of amyloids and confirm that polarization dependence of the observed emission can be correlated with the orientation of fibrils. We show the potential of two-photon excited autofluorescence for resolution of molecular organization of fibrils within amyloid superstructures. This label-free method is compatible with two-photon imaging already applied in investigation of neurodegeneration model in mice.
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