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Fluorescent Probe for Selective Imaging of α-Synuclein Fibrils in Living Cells
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SYSNO ASEP 0542333 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Fluorescent Probe for Selective Imaging of α-Synuclein Fibrils in Living Cells Author(s) Gaur, Pankaj (UOCHB-X) ORCID
Galkin, Maksym (UOCHB-X) ORCID
Kurochka, Andrii (UOCHB-X) ORCID
Ghosh, S. (IN)
Yushchenko, Dmytro A. (UOCHB-X) ORCID, RID
Shvadchak, Volodymyr V. (UOCHB-X) ORCID, RIDSource Title ACS Chemical Neuroscience. - : American Chemical Society - ISSN 1948-7193
Roč. 12, č. 8 (2021), s. 1293-1298Number of pages 6 s. Language eng - English Country US - United States Keywords fluorescence ; α-synuclein ; fibril ; microscopy ; solvatochromic OECD category Biophysics R&D Projects GA19-21318S GA ČR - Czech Science Foundation (CSF) GJ18-06255Y GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support UOCHB-X - RVO:61388963 UT WOS 000643598600002 EID SCOPUS 85104917599 DOI 10.1021/acschemneuro.1c00090 Annotation Plaques of amyloid fibrils composed of neuronal protein α-synuclein are one of the hallmarks of Parkinson’s disease, and their selective imaging is crucial to study the mechanism of its pathogenesis. However, the existing fluorescent probes for amyloids are efficient only in solution and tissue systems, and they are not selective enough for the visualization of amyloid fibrils in living cells. In this study, we present two molecular rotor-based probes RB1 and RB2. These thiazolium probes show affinity to α-synuclein fibrils and turn-on fluorescence response upon interactions. Because of its extended π-conjugation and high rotational degree of freedom, RB1 exhibits a 76 nm red-shift of absorption maxima and 112-fold fluorescence enhancement upon binding to amyloid fibrils. Owing to its strong binding affinity to α-synuclein fibrils, RB1 can selectively stain them in the cytoplasm of living HeLa and SH-SY5Y cells with high optical contrast. RB1 is a cell-permeable and noncytotoxic probe. Taken together, we have demonstrated that RB1 is an amyloid probe with an outstanding absorption red-shift that can be used for intracellular imaging of α-synuclein fibrils. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2022 Electronic address https://doi.org/10.1021/acschemneuro.1c00090
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