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• W3098291263 endingPage "4997" @default.
• W3098291263 startingPage "4989" @default.
• W3098291263 abstract "Amyloidogenic protein aggregation into highly structured fibrils is linked to more than 30 amyloidoses, including several neurodegenerative disorders. Despite significant progress in trying to understand the process of amyloid formation, there is still no cure or effective treatment available. A number of studies involving potential anti-amyloid compounds rely on the use of a fluorescent probe—thioflavin-T—to track the appearance, growth, or disassembly of these cytotoxic aggregates. Despite the wide application of this dye molecule, its interaction with amyloid fibrils is still poorly understood. Recent reports have shown it may possess distinct binding modes and fluorescence intensities based on the conformation of the examined fibrils. In this work, we generate insulin fibrils under four different conditions and attempt to identify distinct conformations using both classic methods, such as atomic force microscopy and Fourier-transform infrared spectroscopy, as well as their ThT binding ability and fluorescence quantum yield. We show that there is a significant variance of ThT fluorescence quantum yields, excitation/emission maxima positions, and binding modes between distinct insulin fibril conformations." @default.
• W3098291263 created "2020-11-23" @default.
• W3098291263 creator A5000531071 @default.
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• W3098291263 date "2020-11-17" @default.
• W3098291263 modified "2023-10-03" @default.
• W3098291263 title "Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics" @default.
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• W3098291263 doi "https://doi.org/10.1021/acs.biomac.0c01178" @default.
• W3098291263 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7739267" @default.
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• W3098291263 hasPublicationYear "2020" @default.
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