Issue 51, 2013
From the journal:

Chemical Communications

Thioflavin-T excimer formation upon interaction with amyloid fibers†

Raimon Sabate,*a   Luis Rodriguez-Santiago,b   Mariona Sodupe,b   Sven J. Saupec  and  Salvador Venturad  

* Corresponding authors

a Institut de Nanociència i nanotecnologia, Departament Fisicoquímica, Universitat de Barcelona, Joan XXIII s/n, E-08028-Barcelona, Spain
E-mail: rsabate@ub.edu
Fax: +34 934035987
Tel: +34 934035986

b Departament de Química, Universitat Autònoma de Barcelona, 08193-Bellaterra, Spain

c Institut de Biochimie et de Génétique Cellulaire, UMR 5095, CNRS – Université de Bordeaux 2, 33077 Bordeaux cedex, France

d Institut de Biotecnologia i Biomedicina, Departament Bioquímica, Universitat Autònoma de Barcelona, 08193-Bellaterra, Spain

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.

Graphical abstract: Thioflavin-T excimer formation upon interaction with amyloid fibers

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Article information

DOI
https://doi.org/10.1039/C3CC42040J
Article type
Communication
Submitted
20 Mar 2013
Accepted
30 Apr 2013
First published
30 Apr 2013

Chem. Commun., 2013,49, 5745-5747

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Thioflavin-T excimer formation upon interaction with amyloid fibers

R. Sabate, L. Rodriguez-Santiago, M. Sodupe, S. J. Saupe and S. Ventura, Chem. Commun., 2013, 49, 5745 DOI: 10.1039/C3CC42040J

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