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

被引：52

作者：

Lindberg, David J. ^{[1
]}

Wenger, Anna ^{[1
,3
]}

Sundin, Elin ^{[2
]}

Wesen, Emelie ^{[1
]}

Westerlund, Fredrik ^{[1
]}

Esbjorner, Elin K. ^{[1
]}

机构：

[1] Chalmers, Div Chem Biol, Dept Biol & Biol Engn, Kemivagen 10, S-41296 Gothenburg, Sweden

[2] Chalmers, Div Chem & Biochem, Dept Chem & Chem Engn, Kemivagen 10, S-41296 Gothenburg, Sweden

[3] Univ Gothenburg, Dept Pathol, Sahlgrenska Canc Ctr, Med Gatan 1F, S-41390 Gothenburg, Sweden

来源：

BIOCHEMISTRY | 2017年 / 56卷 / 16期

基金：

瑞典研究理事会;

关键词：

LINEAR DICHROISM SPECTROSCOPY; MECHANISM; PROBES;

D O I：

10.1021/acs.biochem.7b00035

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Thioflavin-T binds to and detects amyloid fibril's 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.

引用

页码：2170 / 2174

页数：5

共 22 条

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