Thioflavin T fluorescence anisotropy: An alternative technique for the study of amyloid aggregation

被引:51
|
作者
Sabate, Raimon [1 ]
Saupe, Sven J. [1 ]
机构
[1] Univ Bordeaux 2, CNRS, UMR 5095, Inst Biochim & Genet Cellulaires,Lab Genet Mol C, F-33077 Bordeaux, France
关键词
thioflavin T; anisotropy; amyloid; prion; kinetic aggregation; dye binding; fibrillogenesis; Podospora anserina; protein aggregation; fibril polymerisation;
D O I
10.1016/j.bbrc.2007.06.063
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
The process of amyloid polymerisation raises keen interest in particular because of the biomedical impact of this process. A variety of analytical methods have been developed to monitor amyloid formation. Thioflavin T (ThT) is the most commonly used dye for detection of arnyloid aggregation. Nevertheless, ThT fluorescence enhancement is strongly dependent of fibril morphology. In this study using the HET-s prion fibril model, we show that amyloid formation can be monitored by measuring ThT fluorescence anisotropy. Kinetic parameters obtained by this method are identical to those determined by CD spectrometry. We propose that ThT anisotropy represent an interesting, simple and alternative technique to analyze the amyloid formation process. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:135 / 138
页数:4
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