Abstract
Benzthiazole dye thioflavin T (ThT) is widely used for studying amyloid fibrils structure and formation. Nevertheless, till now there is no common opinion concerning molecular mechanisms of ThT binding to amyloid fibrils and the reasons of dramatic increase of its fluorescence quantum yield on incorporation into amyloid fibrils. Our data prove that ThT molecules incorporate in amyloid fibrils in monomeric form and there is no ground to suppose the formation of ThT dimers, eximers, or micelles. It was shown that the increase of quantum yield of ThT incorporated in amyloid fibrils is caused by restriction of benzthiazole and aminobenzene rings torsion fluctuations about each other.
Highlights
Amyloid fibrils are enriched β-sheet a polymeric forms of proteins with the strands perpendicular to the long axis of the fibril [2,3]
Absorption spectrum and molar extinction coefficient of thioflavin T (ThT) in a water solution do not depend on concentration of dye in a range from 10−5 to 10−3 M (Fig. 1A)
There is no ground to suppose the formation of ThT dimers
Summary
Amyloid fibrils are enriched β-sheet a polymeric forms of proteins with the strands perpendicular to the long axis of the fibril [2,3]. Amyloid fibrils structure and formation are studied via the use of specific dyes such as Congo red and thioflavin T (ThT). ThT interaction with amyloid fibrils is highly specific, as this dye does not interact with proteins in native, unfolded and partially folded monomeric forms, oligomers or amorphous aggregates [7,11]. Despite the fact that the number of papers describing the dye application for the analysis of amyloid fibrils is rapidly growing the molecular mechanism of specific dye binding to amyloid fibrils and the reasons of dramatic changes in its fluorescence properties on complexes formation is poorly understood. There are a number of inconsistencies in description of the spectral properties of this dye
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