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A Small‐Molecule FRET Reporter for the Real‐Time Visualization of Cell‐Surface Proteolytic Enzyme Functions
Author(s) -
Mu Jing,
Liu Fang,
Rajab Muhammad Shafiq,
Shi Meng,
Li Shuang,
Goh Chiching,
Lu Lei,
Xu QingHua,
Liu Bin,
Ng Lai Guan,
Xing Bengang
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201407182
Subject(s) - furin , förster resonance energy transfer , biophysics , cleavage (geology) , fluorescence , chemistry , proteolytic enzymes , cell membrane , fluorescence microscope , cell , membrane , live cell imaging , microbiology and biotechnology , enzyme , intracellular , green fluorescent protein , two photon excitation microscopy , biochemistry , biology , gene , paleontology , physics , quantum mechanics , fracture (geology)
Real‐time imaging of cell‐surface‐associated proteolytic enzymes is critical to better understand their performances in both physiological and pathological processes. However, most current approaches are limited by their complexity and poor membrane‐anchoring properties. Herein, we have designed and synthesized a unique small‐molecule fluorescent probe, which combines the principles of passive exogenous membrane insertion and Förster resonance energy transfer (FRET) to image cell‐surface‐localized furin‐like convertase activities. The membrane‐associated furin‐like enzymatic cleavage of the peptide probe leads to an increased fluorescence intensity which was mainly localized on the plasma membrane of the furin‐expressed cells. This small‐molecule fluorescent probe may serve as a unique and reliable reporter for real‐time visualization of endogenous cell‐surfaceassociated proteolytic furin‐like enzyme functions in live cells and tissues using one‐photon and two‐photon microscopy.