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A new twist on PIFE: photoisomerisation-related fluorescence enhancement
PIFE was first used as an acronym for protein-induced fluorescence enhancement, which refers to the increase in fluorescence observed upon the interaction of a fluorophore, such as a cyanine, with a protein. This fluorescence enhancement is due to changes in the rate of cis/trans photoisomerisation....
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cornell University
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980184/ https://www.ncbi.nlm.nih.gov/pubmed/36866225 |
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author | Ploetz, Evelyn Ambrose, Benjamin Barth, Anders Börner, Richard Erichson, Felix Kapanidis, Achillefs N. Kim, Harold D. Levitus, Marcia Lohman, Timothy M. Mazumder, Abhishek Rueda, David S. Steffen, Fabio D. Cordes, Thorben Magennis, Steven W. Lerner, Eitan |
author_facet | Ploetz, Evelyn Ambrose, Benjamin Barth, Anders Börner, Richard Erichson, Felix Kapanidis, Achillefs N. Kim, Harold D. Levitus, Marcia Lohman, Timothy M. Mazumder, Abhishek Rueda, David S. Steffen, Fabio D. Cordes, Thorben Magennis, Steven W. Lerner, Eitan |
author_sort | Ploetz, Evelyn |
collection | PubMed |
description | PIFE was first used as an acronym for protein-induced fluorescence enhancement, which refers to the increase in fluorescence observed upon the interaction of a fluorophore, such as a cyanine, with a protein. This fluorescence enhancement is due to changes in the rate of cis/trans photoisomerisation. It is clear now that this mechanism is generally applicable to interactions with any biomolecule and, in this review, we propose that PIFE is thereby renamed according to its fundamental working principle as photoisomerisation-related fluorescence enhancement, keeping the PIFE acronym intact. We discuss the photochemistry of cyanine fluorophores, the mechanism of PIFE, its advantages and limitations, and recent approaches to turn PIFE into a quantitative assay. We provide an overview of its current applications to different biomolecules and discuss potential future uses, including the study of protein-protein interactions, protein-ligand interactions and conformational changes in biomolecules. |
format | Online Article Text |
id | pubmed-9980184 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Cornell University |
record_format | MEDLINE/PubMed |
spelling | pubmed-99801842023-03-03 A new twist on PIFE: photoisomerisation-related fluorescence enhancement Ploetz, Evelyn Ambrose, Benjamin Barth, Anders Börner, Richard Erichson, Felix Kapanidis, Achillefs N. Kim, Harold D. Levitus, Marcia Lohman, Timothy M. Mazumder, Abhishek Rueda, David S. Steffen, Fabio D. Cordes, Thorben Magennis, Steven W. Lerner, Eitan ArXiv Article PIFE was first used as an acronym for protein-induced fluorescence enhancement, which refers to the increase in fluorescence observed upon the interaction of a fluorophore, such as a cyanine, with a protein. This fluorescence enhancement is due to changes in the rate of cis/trans photoisomerisation. It is clear now that this mechanism is generally applicable to interactions with any biomolecule and, in this review, we propose that PIFE is thereby renamed according to its fundamental working principle as photoisomerisation-related fluorescence enhancement, keeping the PIFE acronym intact. We discuss the photochemistry of cyanine fluorophores, the mechanism of PIFE, its advantages and limitations, and recent approaches to turn PIFE into a quantitative assay. We provide an overview of its current applications to different biomolecules and discuss potential future uses, including the study of protein-protein interactions, protein-ligand interactions and conformational changes in biomolecules. Cornell University 2023-07-10 /pmc/articles/PMC9980184/ /pubmed/36866225 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator. |
spellingShingle | Article Ploetz, Evelyn Ambrose, Benjamin Barth, Anders Börner, Richard Erichson, Felix Kapanidis, Achillefs N. Kim, Harold D. Levitus, Marcia Lohman, Timothy M. Mazumder, Abhishek Rueda, David S. Steffen, Fabio D. Cordes, Thorben Magennis, Steven W. Lerner, Eitan A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title | A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title_full | A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title_fullStr | A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title_full_unstemmed | A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title_short | A new twist on PIFE: photoisomerisation-related fluorescence enhancement |
title_sort | new twist on pife: photoisomerisation-related fluorescence enhancement |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9980184/ https://www.ncbi.nlm.nih.gov/pubmed/36866225 |
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