A new twist on PIFE: photoisomerisation-related fluorescence enhancement

Evelyn Ploetz, Benjamin Ambrose, Anders Barth, Richard Börner, Achillefs N. Kapanidis, Timothy M. Lohman, Fabio D. Steffen, Thorben Cordes*, Steven W. Magennis*, Eitan Lerner*, More Authors

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

5 Citations (Scopus)
152 Downloads (Pure)

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.

Original languageEnglish
Article number012001
Number of pages21
JournalMethods and Applications in Fluorescence
Volume12
Issue number1
DOIs
Publication statusPublished - 2023

Keywords

  • biophysics
  • fluorescence spectroscopy
  • photoisomerisation
  • PIFE
  • single-molecule

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