A New Strategy for Fluorogenic Esterase Probes Displaying Low Levels of Non-specific Hydrolysis

Sungwoo Kim, Hyunjin Kim, Yongdoo Choi, Youngmi Kim

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)9645-9649
Number of pages5
JournalChemistry - A European Journal
Volume21
Issue number27
DOIs
Publication statusPublished - 1 Jun 2015

Keywords

  • BODIPY
  • esterase
  • fluorescent probe
  • fluorogenic substrate
  • turn-on

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