Thioflavin T Fluorescence
Thioflavin T Fluorescence - Related Videos
02:48
Quantifying Bacterial Infection-Induced Amyloids Using Thioflavin T Fluorescence
0 Views •
2025
Source: Balczon, R., et al. Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa. J. Vis. Exp. (2018)This video demonstrates the protocol to quantify amyloids in culture supernatants from pulmonary endothelial cells infected with virulent bacteria, using thioflavin T, a fluorescent dye that binds to amyloid beta-sheet structures. An increase in fluorescence compared to baseline indicates the presence of amyloids in the culture...
04:56
Detection of Aggregation-Prone Behavior in Mutant P53 V157F Breast Cancer Cells Using Multipoint Thioflavin T Fluorescence
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2025
Hs578T breast cancer cells harboring the p53 V157F mutation exhibit significantly higher Thioflavin T fluorescence compared to MCF7 cells, indicating enhanced protein aggregation. Multipoint fluorescence measurements improve detection accuracy and reliability in identifying β-sheet-rich aggregates, underscoring the importance of aggregation-prone p53 mutations in cancer research and the development of therapeutic strategies.
01:21
Thioflavin-S Staining of Amyloid-Beta Aggregation in Cerebral Hypoperfused Mouse Brain Tissue
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2025
MCCH is characterized by reduced blood flow to the brain. This limits oxygen and nutrient supply to the endothelial cell layer of cerebral blood vessels, damaging the cells.
11:23
Lensless Fluorescent Microscopy on a Chip
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Cited by 8 •
2011
A lensless on-chip fluorescent microscopy platform is demonstrated that can image fluorescent objects over an ultra-wide field-of-view of e.g., >0.6-8 cm2 with <4μm resolution using a compressive sampling based decoding algorithm. Such a compact and wide-field fluorescent on-chip imaging modality could be valuable for high-throughput cytometry, rare-cell research and microarray-analysis.
09:22
Introduction to Fluorescence Microscopy
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2023
Fluorescence microscopy is a very powerful analytical tool that combines the magnifying properties of light microscopy with visualization of fluorescence. Fluorescence is a phenomenon that involves absorbance and emission of a small range of light wavelengths by a fluorescent molecule known as a fluorophore. Fluorescence microscopy is accomplished in conjunction with the basic light microscope by the addition of a powerful light source, specialized filters, and a means of fluorescently...
FAQs
In solution, Thioflavin T emits relatively little light because its molecular motion limits efficient fluorescence. When the dye binds to repetitive cross-β-sheet structures in amyloid fibrils, that binding restricts rotation within the molecule. The reduced motion enhances light emission, allowing fluorescence intensity to serve as an optical indicator of amyloid-associated assembly.
The repetitive cross-β-sheet arrangement provides the structural context that enables the strong fluorescence response. This matters because the signal is linked to organized amyloid fibril architecture rather than simply to the presence of protein in a sample. Consequently, changes in fluorescence can reflect the development of fibrillar assemblies during protein aggregation studies.
Researchers can record the fluorescence signal as protein assembly proceeds and examine how it changes over time. Increasing signal provides a way to follow fibril growth, while the resulting time course supports analysis of aggregation kinetics. In vitro, these measurements help quantify the progression of amyloid formation rather than relying only on a final observation.
A basic workflow combines Thioflavin T with a protein system under study and uses optical measurements to track fluorescence during assembly. Researchers can collect readings over the course of the experiment, then relate signal changes to amyloid formation and fibril growth. This approach supports quantitative monitoring of protein aggregation in controlled in vitro studies.
Researchers can compare fluorescence measurements from protein-assembly reactions conducted with and without a test compound. Differences in the signal or its time-dependent progression indicate that the compound alters amyloid formation or fibril growth. This makes the method useful for screening how candidate molecules influence protein assembly, while retaining a direct connection to aggregation kinetics.
In neuroscience, Thioflavin T fluorescence provides a way to study aggregation mechanisms involving amyloid-β, tau, and α-synuclein. By monitoring assembly and fibril growth in vitro, researchers can examine disease-relevant protein behavior and test compounds that modify it. The resulting measurements connect molecular aggregation processes with investigations of neurodegenerative disease mechanisms.