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.
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Cent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R ChinaCent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China
Khusbu, Farjana Yeasmin
Zhou, Xi
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Cent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R ChinaCent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China
Zhou, Xi
Chen, Hanchun
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Cent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R ChinaCent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China
Chen, Hanchun
Ma, Changbei
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Cent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R ChinaCent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China
Ma, Changbei
Wang, Kemin
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Hunan Univ, State Key Lab Chemo Biosensing & Chemometr, Changsha 410081, Hunan, Peoples R ChinaCent S Univ, Sch Life Sci, Changsha 410013, Hunan, Peoples R China