Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils
Abstract Fluorescence of thioflavin T (ThT) is a proven tool for amyloid fibrils study. The correct model of ThT binding to fibrils is crucial to clarify amyloid fibrils structure and mechanism of their formation. Although there are convincing evidences that ThT has molecular rotor nature, implying...
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| Format: | Article |
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Nature Portfolio
2017-05-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-02237-7 |
| _version_ | 1818344282168229888 |
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| author | Anna I. Sulatskaya Andrey V. Lavysh Alexander A. Maskevich Irina M. Kuznetsova Konstantin K. Turoverov |
| author_facet | Anna I. Sulatskaya Andrey V. Lavysh Alexander A. Maskevich Irina M. Kuznetsova Konstantin K. Turoverov |
| author_sort | Anna I. Sulatskaya |
| collection | DOAJ |
| description | Abstract Fluorescence of thioflavin T (ThT) is a proven tool for amyloid fibrils study. The correct model of ThT binding to fibrils is crucial to clarify amyloid fibrils structure and mechanism of their formation. Although there are convincing evidences that ThT has molecular rotor nature, implying it’s binding to fibrils in monomer form, speculations concerning ThT binding to fibrils in aggregated forms appear in literature so far. The elaborated approach for fluorescence intensity correction on the inner filter effects applied to ThT aqueous solutions with a wide range of concentration allowed characterizing ThT excimers fluorescence and showing its difference from that of ThT bound to fibrils. Obtained results experimentally prove the monomer model of ThT binding to amyloid fibrils and demonstrate wide capacity of the used approach in the spectroscopy of other fluorescent dyes for examination of concentration self-quenching and deformation of fluorescence spectra, dye molecules interaction, dimers and excimers formation. |
| first_indexed | 2024-12-13T16:44:00Z |
| format | Article |
| id | doaj.art-06f32f88a9e24f93b7d6feefa91a0255 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-13T16:44:00Z |
| publishDate | 2017-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-06f32f88a9e24f93b7d6feefa91a02552022-12-21T23:38:13ZengNature PortfolioScientific Reports2045-23222017-05-017111110.1038/s41598-017-02237-7Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrilsAnna I. Sulatskaya0Andrey V. Lavysh1Alexander A. Maskevich2Irina M. Kuznetsova3Konstantin K. Turoverov4Laboratory of Structural Dynamics Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of SciencesDepartment of Physics, Yanka Kupala Grodno State UniversityDepartment of Physics, Yanka Kupala Grodno State UniversityLaboratory of Structural Dynamics Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of SciencesLaboratory of Structural Dynamics Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of SciencesAbstract Fluorescence of thioflavin T (ThT) is a proven tool for amyloid fibrils study. The correct model of ThT binding to fibrils is crucial to clarify amyloid fibrils structure and mechanism of their formation. Although there are convincing evidences that ThT has molecular rotor nature, implying it’s binding to fibrils in monomer form, speculations concerning ThT binding to fibrils in aggregated forms appear in literature so far. The elaborated approach for fluorescence intensity correction on the inner filter effects applied to ThT aqueous solutions with a wide range of concentration allowed characterizing ThT excimers fluorescence and showing its difference from that of ThT bound to fibrils. Obtained results experimentally prove the monomer model of ThT binding to amyloid fibrils and demonstrate wide capacity of the used approach in the spectroscopy of other fluorescent dyes for examination of concentration self-quenching and deformation of fluorescence spectra, dye molecules interaction, dimers and excimers formation.https://doi.org/10.1038/s41598-017-02237-7 |
| spellingShingle | Anna I. Sulatskaya Andrey V. Lavysh Alexander A. Maskevich Irina M. Kuznetsova Konstantin K. Turoverov Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils Scientific Reports |
| title | Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| title_full | Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| title_fullStr | Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| title_full_unstemmed | Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| title_short | Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| title_sort | thioflavin t fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils |
| url | https://doi.org/10.1038/s41598-017-02237-7 |
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