A new twist on PIFE
photoisomerisation-related fluorescence enhancement
Evelyn Ploetz (Ludwig Maximilians University)
Benjamin Ambrose (Imperial College London, King’s College London)
Anders Barth (Kavli institute of nanoscience Delft, BN/Cees Dekker Lab)
Richard Börner (University of Applied Science Mittweida)
Achillefs N. Kapanidis (University of Oxford)
Timothy M. Lohman (Washington University School of Medicine)
Fabio D. Steffen (Universitat Zurich)
Thorben Cordes (Ludwig Maximilians University)
Steven W. Magennis (University of Glasgow)
Eitan Lerner (The Hebrew University of Jerusalem)
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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 ofcis/transphotoisomerisation. 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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