NDLI: A New Trend in the Experimental Methodology for the Analysis of the Thioflavin T Binding to Amyloid Fibrils

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A New Trend in the Experimental Methodology for the Analysis of the Thioflavin T Binding to Amyloid Fibrils

Content Provider	Springer Nature Link
Author	Kuznetsova, Irina M. Sulatskaya, Anna I. Uversky, Vladimir N. Turoverov, Konstantin K.
Copyright Year	2012
Abstract	The studies on the determination of the characteristics of the amyloid fibril interaction with the dye were based on the analysis of the dependence of the ThT fluorescence intensity on its concentration in the solution containing the amyloid fibrils. In the present work, we revealed that this intuitive approach provided erroneous data. We propose a new approach which provides a means for characterizing the interaction of thioflavin T (ThT) with amyloid fibrils and for determining the binding stoichiometry and binding constants, absorption spectrum, molar extinction coefficient, and fluorescence quantum yield of the ThT bound to the sites of different binding modes of fibrils. The key point of this approach is sample preparation by equilibrium microdialysis. The efficiency of the proposed approach is demonstrated via the examination of the ThT binding to insulin and Aβ42 fibrils as well as to the native form of the Electrophorus electricus acetylcholinesterase. We show that the peculiarities of ThT interaction with amyloid fibrils depend on the amyloidogenic protein and on the binding mode. This approach is universal and can be used for the analysis of binding mechanism of any dye that interacts with its receptor. Therefore, the proposed approach represents an important addition to the existing arsenal of means for the diagnostics and therapy of the neurodegenerative diseases.
Starting Page	488
Ending Page	498
Page Count	11
File Format	PDF
ISSN	08937648
Journal	Molecular Neurobiology
Volume Number	45
Issue Number	3
e-ISSN	15591182
Language	English
Publisher	Humana Press Inc
Publisher Date	2012-05-17
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Thioflavin T Dye binding Fluorescence quantum yield Equilibrium microdialysis Binding parameters Amyloid fibrils Insulin Aβ42 peptide Acetylcholinesterase Neurosciences Neurobiology Cell Biology Neurology
Content Type	Text
Resource Type	Article
Subject	Neurology Cellular and Molecular Neuroscience

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Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T

Analyzing Thioflavin T Binding to Amyloid Fibrils by an Equilibrium Microdialysis-Based Technique (2012)

Structural Features of Amyloid Fibrils Formed from the Full-Length and Truncated Forms of Beta-2-Microglobulin Probed by Fluorescent Dye Thioflavin T

Analyzing thioflavin T binding to amyloid fibrils by an equilibrium microdialysis-based technique.

Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils

Investigation of the kinetics of insulin amyloid fibrils formation

Interaction of Thioflavin T with Amyloid Fibrils: Fluorescence Quantum Yield of Bound Dye

Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils

New Evidence on a Distinction between Aβ40 and Aβ42 Amyloids: Thioflavin T Binding Modes, Clustering Tendency, Degradation Resistance, and Cross-Seeding

A New Trend in the Experimental Methodology for the Analysis of the Thioflavin T Binding to Amyloid Fibrils

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