Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 56, Issue 48, Pages 15319-15323Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201708428
Keywords
activity-based probes; analytical methods; fluorogenic probes; molecular recognition; monoamine oxidase A
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Funding
- 973 Program [2015CB932001, 2015CB856301]
- NSF of China [21535009, 21435007, 21675159, 21621062]
- Chinese Academy of Science [XDB14030102]
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Monoamine oxidase (MAO) has two isoforms, MAO-A and MAO-B, which show different functions, and thus selective fluorescence imaging is important for biological studies. Currently, however, specific detection of MAO-A remains a great challenge. Herein, we report a new strategy for specific imaging of MAO-A through the design of fluorogenic probes combining the characteristic structure of an inhibitor of the target enzyme along with propylamine as a recognition moiety. The high specificity of our representative probe is demonstrated by imaging MAO-A in different live cells such as SH-SY5Y (high levels of MAO-A) and HepG2 (high levels of MAO-B), and further validated by western blot analyses. The superior specificity of the probe may enable the accurate detection of MAO-A in complex biosystems. Importantly, the use of the characteristic structure of an inhibitor, as demonstrated in this work, may serve as a general strategy to design specific recognition moieties for fluorogenic probes for enzymes.
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