期刊
ANALYTICAL BIOCHEMISTRY
卷 532, 期 -, 页码 83-86出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2017.06.007
关键词
Amyloid; Thioflavin T; Fluorescence; Islet amyloid polypeptide; Amyloid-beta peptide
资金
- Natural Sciences and Engineering Research Council of Canada (NSERC) [418614]
- Fonds de Recherche du Quebec-Nature et technologies (FRQNT) [180394]
The most frequent method to monitor amyloid formation relies on the fluorescence of thioflavin T (ThT). The present study reports a novel factor of irreproducibility in ThT kinetic assays performed in micro plate. Discrepancies among kinetics of amyloid assembly, performed under quiescent conditions, were associated with the frequency of fluorescence measurement. Evaluating self-assembly of the islet amyloid polypeptide at short intervals hastened its fibrillization. This observation was confirmed by transmission electron microscopy, circular dichroism spectroscopy and 8-anilino-1-naphthalenesulfonic acid fluorescence. This effect, attributed to agitation during microplate displacements between fluorescence measurements, reinforces the importance of a better standardization in amyloid formation assays. (C) 2017 Elsevier Inc. All rights reserved.
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