Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction

Lindberg, David,1986Chalmers tekniska högskola,Chalmers University of Technology (författare)

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.

Wenger, Anna,1991Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)annawen (författare)
Sundin, Elin,1992Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)suelin (författare)
Lindahl Wesén, Emelie,1989Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)emelin (författare)
Westerlund, Fredrik,1978Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)fredrikw (författare)
Esbjörner Winters, Elin,1978Chalmers tekniska högskola,Chalmers University of Technology(Swepub:cth)eline (författare)
Chalmers tekniska högskola (creator_code:org_t)

Ingår i:Biochemistry: American Chemical Society (ACS)56:16, s. 2170-21741520-49950006-2960

Av författaren/redakt...: Lindberg, David, ...; Wenger, Anna, 19 ...; Sundin, Elin, 19 ...; Lindahl Wesén, E ...; Westerlund, Fred ...; Esbjörner Winter ...

Om ämnet

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.