Detection and Characterization of Aggregates, Prefibrillar Amyloidogenic Oligomers, and Protofibrils Using Fluorescence Spectroscopy
TLDR
A novel pathway for generation of prefibrillar aggregates of TTR is explored, which provides important insight into TTR misfolding and suggests that unbound ThT dramatically increases its fluorescence quantum yield when bound to amyloid fibrils; however, the mechanism behind this property is unknown.About:
This article is published in Biophysical Journal.The article was published on 2005-06-01 and is currently open access. It has received 316 citations till now. The article focuses on the topics: Amyloid disease & Amyloid.read more
Citations
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Journal ArticleDOI
Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Matthew Biancalana,Shohei Koide +1 more
TL;DR: Recent progress in the understanding of ThT-fibril interactions at an atomic resolution is reviewed to offer guidance for designing the next generation of amyloid assembly diagnostics, inhibitors, and therapeutics.
Journal ArticleDOI
Extrinsic fluorescent dyes as tools for protein characterization.
TL;DR: The intention of this review is to give an overview of available extrinsic dyes, explain their spectral properties, and show illustrative examples of their various applications in protein characterization.
Journal ArticleDOI
Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
Minna Groenning,Minna Groenning +1 more
TL;DR: Increased understanding of present molecular probes as well as development of new probes are of utmost importance for development of strategies to control amyloid formation and overcome neurodegenerative disorders.
Journal ArticleDOI
Environment-sensitive behavior of fluorescent molecular rotors
TL;DR: This review presents the pertinent theories of the rotor-solvent interaction on the molecular level and how this interaction leads to the viscosity-sensitive behavior of molecular rotors.
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Thioflavin T as a molecular rotor: fluorescent properties of thioflavin T in solvents with different viscosity.
Vitali I. Stsiapura,A. A. Maskevich,V. A. Kuzmitsky,Vladimir N. Uversky,Irina M. Kuznetsova,Konstantin K. Turoverov +5 more
TL;DR: The photophysical model successfully explains the fluorescent properties of ThT in solvents with different viscosities and supports the idea that the reason for the characteristic increase in the ThT fluorescence intensity accompanying its incorporation into the amyloid fibrils is determined by the rigidity of the dye environment.
References
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Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
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Diffusible, nonfibrillar ligands derived from Aβ1–42 are potent central nervous system neurotoxins
Mary P. Lambert,A. K. Barlow,Brett A. Chromy,C. Edwards,R. Freed,M. Liosatos,Todd E. Morgan,Irina Rozovsky,Barbara L. Trommer,Kirsten L. Viola,Pat Wals,Chuan Zhang,Caleb E. Finch,Grant A. Krafft,William L. Klein +14 more
TL;DR: It is hypothesized that impaired synaptic plasticity and associated memory dysfunction during early stage Alzheimer's disease and severe cellular degeneration and dementia during end stage could be caused by the biphasic impact of Abeta-derived diffusible ligands acting upon particular neural signal transduction pathways.
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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.
TL;DR: Thioflavine T associates rapidly with aggregated fibrils of the synthetic β/A4‐derived peptides β( 1–28) and β(1–40), giving rise to a new excitation maximum at 450 nm and enhanced emission at 482 nm, as opposed to the 385 nm and 445 nm of the free dye.
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Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe.
Gennady V. Semisotnov,N. A. Rodionova,O. I. Razgulyaev,Vladimir N. Uversky,A. F. Gripas,R. I. Gilmanshin +5 more
TL;DR: Binding of the hydrophobia fluorescent probe, 1‐anilino‐naphthalene‐8‐sulfonate (ANS), to synthetic polypeptides and proteins with a different structural organization has been studied and it has been shown that ANS has a much stronger affinity to the protein “molten globule” state.
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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.
TL;DR: Fluorescence intensity in the presence of a constant amount of amyloid fibrils reached a plateau with increase in the thioflavine T concentration, and the fluorescence was considerably diminished when structure of the amyloids fibril was disrupted by guanidine-HCl treatment.