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Title: Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR
Authors: Iwakawa, Naoto
Morimoto, Daichi  kyouindb  KAKEN_id  orcid (unconfirmed)
Walinda, Erik  kyouindb  KAKEN_id  orcid (unconfirmed)
Kawata, Yasushi
Shirakawa, Masahiro
Sugase, Kenji  kyouindb  KAKEN_id  orcid (unconfirmed)
Author's alias: 岩川, 直都
森本, 大智
白川, 昌宏
菅瀬, 謙治
Keywords: amyloid fibrils
thioflavin T
molecular interactions
real-time observation
Issue Date: 28-Oct-2017
Publisher: MDPI AG
Journal title: International Journal of Molecular Sciences
Volume: 18
Issue: 11
Thesis number: 2271
Abstract: Amyloid fibril formation is associated with numerous neurodegenerative diseases. To elucidate the mechanism of fibril formation, the thioflavin T (ThT) fluorescence assay is widely used. ThT is a fluorescent dye that selectively binds to amyloid fibrils and exhibits fluorescence enhancement, which enables quantitative analysis of the fibril formation process. However, the detailed binding mechanism has remained unclear. Here we acquire real-time profiles of fibril formation of superoxide dismutase 1 (SOD1) using high-sensitivity Rheo-NMR spectroscopy and detect weak and strong interactions between ThT and SOD1 fibrils in a time-dependent manner. Real-time information on the interaction between ThT and fibrils will contribute to the understanding of the binding mechanism of ThT to fibrils. In addition, our method provides an alternative way to analyze fibril formation.
Rights: © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
DOI(Published Version): 10.3390/ijms18112271
Appears in Collections:Journal Articles

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