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Binding of Thioflavin-T to Amyloid Fibrils Leads to Fluorescence Self-Quenching and Fibril Compaction.
Lindberg, David J; Wenger, Anna; Sundin, Elin; Wesén, Emelie; Westerlund, Fredrik; Esbjörner, Elin K.
Afiliação
  • Lindberg DJ; Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
  • Wenger A; Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
  • Sundin E; Division of Chemistry and Biochemistry, Department of Chemistry and Chemical Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
  • Wesén E; Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
  • Westerlund F; Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
  • Esbjörner EK; Division of Chemical Biology, Department of Biology and Biological Engineering, Chalmers University of Technology , Kemivägen 10, 412 96 Gothenburg, Sweden.
Biochemistry ; 56(16): 2170-2174, 2017 04 25.
Article em En | MEDLINE | ID: mdl-28402629
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tiazóis / Amiloide Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tiazóis / Amiloide Idioma: En Ano de publicação: 2017 Tipo de documento: Article