Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction
Journal article, 2017

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.

Author

David Lindberg

Chalmers, Biology and Biological Engineering, Chemical Biology

Anna Wenger

Chalmers, Biology and Biological Engineering

Elin Sundin

Chalmers, Chemistry and Chemical Engineering, Chemistry and Biochemistry, Physical Chemistry

Emelie Lindahl Wesén

Chalmers, Biology and Biological Engineering, Chemical Biology

Fredrik Westerlund

Chalmers, Biology and Biological Engineering, Chemical Biology

Elin Esbjörner Winters

Chalmers, Biology and Biological Engineering, Chemical Biology

Biochemistry

0006-2960 (ISSN) 1520-4995 (eISSN)

Vol. 56 16 2170-2174

Subject Categories

Physical Chemistry

Biochemistry and Molecular Biology

DOI

10.1021/acs.biochem.7b00035

More information

Created

10/7/2017