ArticleThe journal of physical chemistry letters2024
Thioflavin T─a Reporter of Microviscosity in Protein Aggregation Process: The Study Case of α-Synuclein.
Article in The journal of physical chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Hyphenated Mass Spectrometry-Based Strategies for Characterizing Oligomers of α‑Synuclein in Parkinson's Disease.ACS central science · 2026Article
- Article
- Boosting AMPs' Power: From Structural Engineering to Nanotechnology-Based Delivery.Molecules (Basel, Switzerland) · 2025Review
- Thioflavin T Lasing Probe for Mucin Detection in Simulated Tears as a Targeting Strategy for Brain Tumors.ACS chemical neuroscience · 2025Article
- Overexpression inFrontiers in cellular and infection microbiology · 2025Article
- Design and Characterization of Antibacterial Peptide Nanofibrils as Components of Composites for Biomaterial Applications.Current protein & peptide science · 2025Article
- Quantification of Rapid Cooling of Glycerol/Water Solutions Based on Photoluminescence from Thioflavin T.The journal of physical chemistry. B · 2024Article
- Cavity Lasing of Thioflavin T in the Condensed Phase for Discrimination between Surface Interaction and β-Sheet Groove Binding in Alzheimer-Linked Peptides.The journal of physical chemistry letters · 2024Article
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5 authors.
Funding
Abstract
Thioflavin T (ThT) informed microviscosity changes can be used to monitor protein aggregation. Steady-state, time-resolved and lasing spectroscopy were used to detect transient states in α-synuclein - a protein associated with Parkinson's disease. The major focus was on the nucleation phase, where conventional ThT fluorescence assay lacks appropriate sensitivity to detect early stage oligomers. Instead, lasing spectroscopy and lasing threshold parameters, in particular, were sensitive to detecting protein oligomers. Through lasing spectroscopy, a change in microviscosity correlating with the stages of protein aggregation was observed at two wavelengths 405 and 440 nm. The two wavelengths are associated with free dye molecules and β-sheet bound ThT molecules. This provides a perspective on elucidating the early formed protein aggregation, a critical aspect in understanding the pathogenesis of neurodegenerative diseases. The insights from the presented study shows the potential of using lasing spectroscopy as a sensitive tool in studying protein aggregation dynamics.
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