1380500-86-6Relevant articles and documents
Cyanine compound containing tetrazine unit and preparation method and application thereof
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, (2021/06/09)
The invention provides a cyanine compound containing a tetrazine unit, a preparation method of the cyanine compound and application of the cyanine compound to near-infrared fluorescence labeling of tumor cells by utilizing a biological orthogonal reaction
Detecting hypoxia: In vitro using 18F-pretargeted IEDDA click chemistry in live cells
Aboagye, Eric O.,Allott, Louis,Barnes, Chris,Braga, Marta,Brickute, Diana,Carroll, Laurence,Chen, Cen,Leung, Sau Fung Jacob,Wang, Ning
, p. 20335 - 20341 (2021/06/28)
We have exemplified a pretargeted approach to interrogate hypoxia in live cells using radioactive bioorthogonal inverse electron demand Diels-Alder (IEDDA) click chemistry. Our novel 18F-tetrazine probe ([18F]FB-Tz) and 2-nitroimidazole-based TCO targeting molecule (8) showed statistically significant (P a 60 min incubation of [18F]FB-Tz. This is the first time that an intracellularly targeted small-molecule for IEDDA click has been used in conjunction with a radioactive reporter molecule in live cells and may be a useful tool with far-reaching applicability for a variety of applications. This journal is
Bioorthogonal "labeling after Recognition" Affording an FRET-Based Luminescent Probe for Detecting and Imaging Caspase-3 via Photoluminescence Lifetime Imaging
Dai, Peiling,Huang, Wei,Liu, Shujuan,Song, Linna,Wang, Ling,Wang, Yun,Wu, Qi,Zhang, Kenneth Yin,Zhao, Qiang,Zhu, Hengyu
supporting information, p. 1057 - 1064 (2020/02/20)
Bis-labeling with a luminescent energy donor/acceptor pair onto biological substrates affords probes which give FRET readouts for the detection of interaction partners. However, the covalently bound luminophores bring about steric hindrance and nonspecific interaction, which probably perturb the biological recognition. Herein, we designed a highly sensitive and specific "labeling after recognition" sensing approach, where luminophore labeling occurred after the biological recognition. Taking the cutting enzyme caspase-3 as an example, we demonstrated the detection of its catalytic activity in solution and apoptotic cells using the tetrapeptide motif Asp-Glu-Val-Asp (DEVD) as the cleavable substrate, and an iridium(III) complex and a rhodamine derivative as the energy donor/acceptor pair. The DEVD tetrapeptide was modified with an azide and a GK-norbornylene groups at the amino and carboxyl terminuses, respectively, which allowed donor/acceptor bis-labeling via two independent catalysis-free bioorthogonal reactions. The phosphorescence lifetime of the iridium(III) complex was quenched upon bis-labeling owing to the intracellular FRET to the rhodamine derivative, and significantly elongated upon the peptide being catalytically cleaved by caspase-3. Interestingly, the sensitivity and efficiency of the lifetime responses were much higher in the "labeling after recognition" sensing approach. Molecular docking analysis showed that the steric hindrance and nonspecific interactions partially inhibited the biological recognition of the DEVD substrate by caspase-3. The imaging of the catalytic activity of caspase-3 in apoptotic cells was demonstrated via photoluminescence lifetime imaging microscopy. Lifetime analysis not only confirmed the occurrence of intracellular bioorthogonal bis-labeling and catalytic cleavage, but also showed the extent to which the two dynamic processes occurred.
