Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction
Artikel i vetenskaplig tidskrift, 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.

Författare

David Lindberg

Chalmers, Biologi och bioteknik, Kemisk biologi

Anna Wenger

Chalmers, Biologi och bioteknik

Elin Sundin

Kemi och kemiteknik, Kemi och biokemi, Fysikalisk kemi

Emelie Lindahl Wesén

Chalmers, Biologi och bioteknik, Kemisk biologi

Fredrik Westerlund

Chalmers, Biologi och bioteknik, Kemisk biologi

Elin Esbjörner Winters

Chalmers, Biologi och bioteknik, Kemisk biologi

Biochemistry

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

Vol. 56 2170-2174

Ämneskategorier

Fysikalisk kemi

Biokemi och molekylärbiologi

DOI

10.1021/acs.biochem.7b00035