A new twist on PIFE: photoisomerisation-related fluorescence enhancement

Evelyn Ploetz; Benjamin Ambrose; Anders Barth; Richard Börner; Felix Erichson; Achillefs N. Kapanidis; Harold D. Kim; Marcia Levitus; Timothy M. Lohman; Abhishek Mazumder; David S. Rueda; Fabio D. Steffen; Thorben Cordes; Steven W. Magennis; Eitan Lerner

doi:10.1088/2050-6120/acfb58

A new twist on PIFE: photoisomerisation-related fluorescence enhancement

Evelyn Ploetz, Benjamin Ambrose, Anders Barth, Richard Börner, Felix Erichson, Achillefs N. Kapanidis, Harold D. Kim, Marcia Levitus, Timothy M. Lohman, Abhishek Mazumder, David S. Rueda, Fabio D. Steffen, Thorben Cordes, Steven W. Magennis, Eitan Lerner

Molecular Sciences, School of (SMS)

Research output: Contribution to journal › Review article › peer-review

3 Scopus citations

Abstract

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. 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 turning 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.

Original language	English (US)
Article number	012001
Journal	Methods and applications in fluorescence
Volume	12
Issue number	1
DOIs	https://doi.org/10.1088/2050-6120/acfb58
State	Published - Jan 1 2024

Keywords

PIFE
biophysics
fluorescence spectroscopy
photoisomerisation
single-molecule

ASJC Scopus subject areas

Atomic and Molecular Physics, and Optics
Instrumentation
General Materials Science
Spectroscopy

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10.1088/2050-6120/acfb58

Cite this

Ploetz, E., Ambrose, B., Barth, A., Börner, R., Erichson, F., Kapanidis, A. N., Kim, H. D., Levitus, M., Lohman, T. M., Mazumder, A., Rueda, D. S., Steffen, F. D., Cordes, T., Magennis, S. W., & Lerner, E. (2024). A new twist on PIFE: photoisomerisation-related fluorescence enhancement. Methods and applications in fluorescence, 12(1), Article 012001. https://doi.org/10.1088/2050-6120/acfb58

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abstract = "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. 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 turning 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.",

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author = "Evelyn Ploetz and Benjamin Ambrose and Anders Barth and Richard B{\"o}rner and Felix Erichson and Kapanidis, {Achillefs N.} and Kim, {Harold D.} and Marcia Levitus and Lohman, {Timothy M.} and Abhishek Mazumder and Rueda, {David S.} and Steffen, {Fabio D.} and Thorben Cordes and Magennis, {Steven W.} and Eitan Lerner",

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doi = "10.1088/2050-6120/acfb58",

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T2 - photoisomerisation-related fluorescence enhancement

AU - Ploetz, Evelyn

AU - Ambrose, Benjamin

AU - Barth, Anders

AU - Börner, Richard

AU - Erichson, Felix

AU - Kapanidis, Achillefs N.

AU - Kim, Harold D.

AU - Levitus, Marcia

AU - Lohman, Timothy M.

AU - Mazumder, Abhishek

AU - Rueda, David S.

AU - Steffen, Fabio D.

AU - Cordes, Thorben

AU - Magennis, Steven W.

AU - Lerner, Eitan

PY - 2024/1/1

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N2 - 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. 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 turning 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.

AB - 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. 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 turning 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.

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KW - photoisomerisation

KW - single-molecule

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A new twist on PIFE: photoisomerisation-related fluorescence enhancement

Abstract

Keywords

ASJC Scopus subject areas

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