ArticleAnalytical chemistry2022
Label-Free Characterization of Amyloids and Alpha-Synuclein Polymorphs by Exploiting Their Intrinsic Fluorescence Property.
Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026Article
- Deep Learning for Fluorescence Lifetime Predictions Enables High-Throughput In Vivo Imaging.Journal of the American Chemical Society · 2025Article
- Crystallization of L-Cysteine in Heavy Water Induces Intrinsic Fluorescence.Angewandte Chemie (International ed. in English) · 2025Article
- Understanding the Protective Effect of Liquid Nitrogen Freezing on Crayfish Quality During Transportation and Storage.Foods (Basel, Switzerland) · 2025Article
- Local Ionic Conditions Modulate the Aggregation Propensity and Influence the Structural Polymorphism of α-Synuclein.Journal of the American Chemical Society · 2025Article
- One-Step Solvothermal Synthesis of Carbon Dots for Rapid and Accurate Determination of Hemin Content.Molecules (Basel, Switzerland) · 2025Article
- In Vitro Cell Model Investigation of Alpha-Synuclein Aggregate Morphology Using Spectroscopic Imaging.International journal of molecular sciences · 2024Article
- A Comprehensive Analysis of the Intrinsic Visible Fluorescence Emitted by Peptide/Protein Amyloid-like Assemblies.International journal of molecular sciences · 2023Review
- Solvent-Driven Self-Organization ofLangmuir : the ACS journal of surfaces and colloids · 2023Article
- Intrinsic fluorescence of nucleobase crystals.Nanoscale advances · 2023Article
- Dissecting aggregation and seeding dynamics of α-Syn polymorphs using the phasor approach to FLIM.Communications biology · 2022Article
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7 authors.
Funding
Abstract
Conventional in vitro aggregation assays often involve tagging with extrinsic fluorophores, which can interfere with aggregation. We propose the use of intrinsic amyloid fluorescence lifetime probed using two-photon excitation and represented by model-free phasor plots as a label-free assay to characterize the amyloid structure. Intrinsic amyloid fluorescence arises from the structured packing of β-sheets in amyloids and is independent of aromatic-based fluorescence. We show that different amyloids [i.e., α-Synuclein (αS), β-Lactoglobulin (βLG), and TasA] and different polymorphic populations of αS (induced by aggregation in salt-free and salt buffers mimicking the intra-/extracellular environments) can be differentiated by their unique fluorescence lifetimes. Moreover, we observe that disaggregation of the preformed fibrils of αS and βLG leads to increased fluorescence lifetimes, distinct from those of their fibrillar counterparts. Our assay presents a medium-throughput method for rapid classification of amyloids and their polymorphs (the latter of which recent studies have shown lead to different disease pathologies) and for testing small-molecule inhibitory compounds.
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