Abstract
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.
Funder
H2020 Marie Sklodowska-Curie Actions
European Social Funds and the Saxon Government as REACT-EU-research group
National Institute of General Medical Sciences
National Science Foundation
Bundesministerium für Bildung und Forschung
Deutsche Forschungsgemeinschaft
Wellcome Trust
Biotechnology and Biological Sciences Research Council
Israel Science Foundation
Subject
Spectroscopy,General Materials Science,Instrumentation,Atomic and Molecular Physics, and Optics
Cited by
2 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献