Native Chemical Ligation-Based Fluorescent Probes for Cysteine and Aminopeptidase N Using meso-thioester-BODIPY
- Authors
- Lee, Uisung; Kim, Tae-Il; Jeon, Sungjin; Luo, Yongyang; Cho, Siyoung; Bae, Jeehyeon; Kim, Youngmi
- Issue Date
- 1-Sep-2021
- Publisher
- WILEY-V C H VERLAG GMBH
- Keywords
- aminopeptidase N; biothiols; BODIPY; cysteine; fluorescent Probe
- Citation
- CHEMISTRY-A EUROPEAN JOURNAL, v.27, no.49, pp 12545 - 12551
- Pages
- 7
- Journal Title
- CHEMISTRY-A EUROPEAN JOURNAL
- Volume
- 27
- Number
- 49
- Start Page
- 12545
- End Page
- 12551
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/51288
- DOI
- 10.1002/chem.202101990
- ISSN
- 0947-6539
1521-3765
- Abstract
- meso-Carboxyl-BODIPY responds to small electronic changes resulting from acyl substitution reactions with a marked change in fluorescence. Herein, the minute changes that accompany the thioester to amide conversion encountered in native chemical ligation (NCL) are exploited in the construction of fluorescent "turn-on" probes. Two fluorogenic probes, 1 a and 4, derived from a meso-thioester-BODIPY scaffold, were designed for the selective detection of cysteine (1 a) and aminopeptidase N (4), respectively. The aromatic (1 a) and aliphatic (4) thioesters of meso-carboxyl-BODIPY are nonfluorescent. However, specific analyte-induced conversion to the meso-amide derivative caused significant spectral changes and a dramatic fluorescence enhancement. Probe 1 a exhibited a large fluorescence "turn-on" response with high selectivity toward cysteine via a tandem NCL reaction. Probe 4 was successfully applied to the monitoring and imaging of endogenous aminopeptidase N in live cancer cells.
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