Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils

Risultato della ricerca: Articlepeer review

4 Citazioni (Scopus)


The formation of amyloid structures has traditionally been related to human neurodegenerative pathologies and, in recent years, the interest in these highly stable nanostructures was extended to biomaterial sciences. A common method to monitor amyloid growth is the analysis of Thioflavin T fluorescence. The use of this highly selective dye, diffused worldwide, allows mechanistic studies of supramolecular assemblies also giving back important insight on the structure of these aggregates. Here we present experimental evidence of self-quenching effect of Thioflavin T in presence of amyloid fibrils. A significant reduction of fluorescence lifetime of this dye which is not related to the properties of analyzed amyloid structures is found. This result is achieved by coupling Fluorescence Lifetime Imaging Microscopy with phasor approach as suitable model-free methods and constitute a serious warning that have to be taken in account if is dye is used for quantitative studies.
Lingua originaleEnglish
pagine (da-a)1-6
Numero di pagine6
RivistaMicroscopy Research and Technique
Stato di pubblicazionePublished - 2020

All Science Journal Classification (ASJC) codes

  • ???subjectarea.asjc.2700.2702???
  • ???subjectarea.asjc.2700.2722???
  • ???subjectarea.asjc.3100.3105???
  • ???subjectarea.asjc.3600.3607???


Entra nei temi di ricerca di 'Phasor-FLIM analysis of Thioflavin T self-quenching in Concanavalin amyloid fibrils'. Insieme formano una fingerprint unica.

Cita questo