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Int. J. Mol. Sci. 2017, 18(11), 2271; https://doi.org/10.3390/ijms18112271

Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR

1
Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-ku, Kyoto 615-8510, Japan
2
Department of Molecular and Cellular Physiology, Graduate School of Medicine, Kyoto University, Yoshida Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan
3
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyama-cho Minami, Tottori 680-8552, Japan
*
Author to whom correspondence should be addressed.
Received: 2 October 2017 / Revised: 25 October 2017 / Accepted: 25 October 2017 / Published: 28 October 2017
(This article belongs to the Collection Proteins and Protein-Ligand Interactions)
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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. View Full-Text
Keywords: amyloid fibrils; thioflavin T; molecular interactions; Rheo-NMR; real-time observation; SOD1 amyloid fibrils; thioflavin T; molecular interactions; Rheo-NMR; real-time observation; SOD1
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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).

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Iwakawa, N.; Morimoto, D.; Walinda, E.; Kawata, Y.; Shirakawa, M.; Sugase, K. Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR. Int. J. Mol. Sci. 2017, 18, 2271.

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