A New Strategy for Fluorogenic Esterase Probes Displaying Low Levels of Non‐specific Hydrolysis |
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| Authors: | Sungwoo Kim Hyunjin Kim Dr. Yongdoo Choi Prof. Youngmi Kim |
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| Affiliation: | 1. Department of Chemistry, Institute of Nanosensor and Biotechnology, Dankook University, 152 Jukjeon‐ro, Suji‐gu, Yongin‐si, Gyeonggi‐do, 448‐701 (Korea), Fax: (+82)?31‐8005‐3148;2. Molecular Imaging & Therapy Branch, National Cancer Center, 323 Ilsan‐ro, Goyang‐si, Gyeonggi‐do, 410‐769 (Korea) |
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| 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. |
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| Keywords: | BODIPY esterase fluorescent probe fluorogenic substrate turn‐on |
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