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Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction
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- Lindberg, David, 1986 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Wenger, Anna, 1991 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- Sundin, Elin, 1992 (author)
- Chalmers tekniska högskola,Chalmers University of Technology
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- 2017-04-17
- 2017
- English.
- In: Biochemistry. - : American Chemical Society (ACS). - 1520-4995 .- 0006-2960. ; 56:16, s. 2170-2174
- Journal article (peer-reviewed)
Abstract
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- Thioflavin-T binds to and detects amyloid fibrils via fluorescence enhancement. Using a combination of linear dichroism and fluorescence spectroscopies, we report that the relation between the emission intensity and binding of thioflavin-T to insulin fibrils is nonlinear and discuss this in relation to its use in kinetic assays. We demonstrate, from fluorescence lifetime recordings, that the nonlinearity is due to thioflavin-T being sensitive to self-quenching. In addition, thioflavin-T can induce fibril compaction but not alter fibril structure. Our work underscores the photophysical complexity of thioflavin-T and the necessity of calibrating the linear range of its emission response for quantitative in vitro studies.
Subject headings
- NATURVETENSKAP -- Kemi -- Fysikalisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Physical Chemistry (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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