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A New Strategy for Fluorogenic Esterase Probes Displaying Low Levels of Non‐specific Hydrolysis
Author(s) -
Kim Sungwoo,
Kim Hyunjin,
Choi Yongdoo,
Kim Youngmi
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201501127
Subject(s) - esterase , fluorophore , bodipy , hydrolysis , chemistry , fluorescence , reactivity (psychology) , enzyme , carboxylate , extracellular , enzymatic hydrolysis , biochemistry , chromatography , medicine , physics , alternative medicine , pathology , quantum mechanics
A new design for fluorescence probes of esterase activity that features a carboxylate‐side pro‐fluorophore is demonstrated with boron dipyrromethene (BODIPY)‐based probes 1 a and 1 b . Because the design relies on the enzyme‐catalyzed hydrolysis of an ester group that is not electronically activated, these probes exhibit a stability to background hydrolysis that is far superior to classical alcohol‐side profluorophore‐based probes, large signal‐to‐noise ratios, reduced sensitivity to pH variations, and high enzymatic reactivity. The utility of probe 1 a was established with a real‐time fluorescence imaging experiment of endogenous esterase activity that does not require washing of the extracellular medium.