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Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils
Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer’s, Parkinson’s, prion diseases, etc. However, the possible effect of these probes on amyloid fib...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7009331/ https://www.ncbi.nlm.nih.gov/pubmed/32008441 http://dx.doi.org/10.1080/19336896.2020.1720487 |
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author | Sulatsky, M. I. Sulatskaya, A. I. Povarova, O. I. Antifeeva, Iu. A. Kuznetsova, I. M. Turoverov, K. K. |
author_facet | Sulatsky, M. I. Sulatskaya, A. I. Povarova, O. I. Antifeeva, Iu. A. Kuznetsova, I. M. Turoverov, K. K. |
author_sort | Sulatsky, M. I. |
collection | PubMed |
description | Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer’s, Parkinson’s, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study. |
format | Online Article Text |
id | pubmed-7009331 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-70093312020-02-24 Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils Sulatsky, M. I. Sulatskaya, A. I. Povarova, O. I. Antifeeva, Iu. A. Kuznetsova, I. M. Turoverov, K. K. Prion Research Paper Fluorescent probes thioflavin T (ThT) and 1-anilino-8-naphthalene sulfonate (ANS) are widely used to study amyloid fibrils that accumulate in the body of patients with serious diseases, such as Alzheimer’s, Parkinson’s, prion diseases, etc. However, the possible effect of these probes on amyloid fibrils is not well understood. In this work, we investigated the photophysical characteristics, structure, and morphology of mature amyloid fibrils formed from two model proteins, insulin and lysozyme, in the presence of ThT and ANS. It turned out that ANS affects the secondary structure of amyloids (shown for fibrils formed from insulin and lysozyme) and their fibers clusterization (valid for lysozyme fibrils), while ThT has no such effects. These results confirm the differences in the mechanisms of these dyes interaction with amyloid fibrils. Observed effect of ANS was explained by the electrostatic interactions between the dye molecule and cationic groups of amyloid-forming proteins (unlike hydrophobic binding of ThT) that induce amyloids conformational changes. This interaction leads to weakening repulsion between positive charges of amyloid fibrils and can promote their clusterization. It was shown that when fibrillogenesis conditions and, consequently, fibrils structure is changing, as well as during defragmentation of amyloids by ultrasonication, the influence of ANS to amyloids does not change, which indicates the universality of the detected effects. Based on the obtained results, it was concluded that ANS should be used cautiously for the study of amyloid fibrils, since this fluorescence probe have a direct effect on the object of study. Taylor & Francis 2020-02-03 /pmc/articles/PMC7009331/ /pubmed/32008441 http://dx.doi.org/10.1080/19336896.2020.1720487 Text en © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Sulatsky, M. I. Sulatskaya, A. I. Povarova, O. I. Antifeeva, Iu. A. Kuznetsova, I. M. Turoverov, K. K. Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title | Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title_full | Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title_fullStr | Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title_full_unstemmed | Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title_short | Effect of the fluorescent probes ThT and ANS on the mature amyloid fibrils |
title_sort | effect of the fluorescent probes tht and ans on the mature amyloid fibrils |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7009331/ https://www.ncbi.nlm.nih.gov/pubmed/32008441 http://dx.doi.org/10.1080/19336896.2020.1720487 |
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