Published in
Royal Society of Chemistry, Chemical Communications, 51(49), p. 5745, 2013
DOI: 10.1039/c3cc42040j
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Thioflavin-T excimer formation upon interaction with amyloid fibers.
Journal article published in 2013 by
Raimon Sabate 
,
Luis Rodriguez-Santiago ,
Mariona Sodupe,
Sven J. Saupe,
Salvador Ventura ,
,
Luis Rodriguez-Santiago ,
Mariona Sodupe,
Sven J. Saupe,
Salvador Ventura ,
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Abstract
The molecular mechanism of the Thioflavin-T (Th-T) binding to amyloids remains unknown. By combining experimental analysis of Th-T excitation and emission spectra with theoretical calculations we suggest that Th-T fluorescence changes upon interaction with amyloids may arise from the formation of an excimer with an oblique angle of ∼120 degrees.