title: Ultrafast fluorescence spectroscopy reveals a dominant weakly-emissive population of fibril bound thioflavin-T.
abstract: In this communication, using sub-picosecond resolved fluorescence upconversion spectroscopy, we discover that despite a large fluorescence enhancement observed for thioflavin-T in insulin fibrils, the majority of fibril bound thioflavin-T undergoes efficient ultrafast conformational relaxation, and thus does not contribute to the characteristic fluorescence enhancement.
authors.affiliation: Radiation & Photochemistry Division, Bhabha Atomic Research Centre, Mumbai 400085, India. prabhatk@barc.gov.in snath@barc.gov.in.
authors.forename: Prabhat K
authors.initials: PK
authors.lastname: Singh
authors.forename: Aruna K
authors.initials: AK
authors.lastname: Mora
authors.forename: Sukhendu
authors.initials: S
authors.lastname: Nath
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D052160:Benzothiazoles; D005456:Fluorescent Dyes / Q000737:chemistry*; D007328:Insulin / Q000737:chemistry*; D015394:Molecular Structure; D011485:Protein Binding; D012680:Sensitivity and Specificity; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013844:Thiazoles / Q000737:chemistry*
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D007328:Insulin; D013844:Thiazoles; C009462:thioflavin T