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Issue 3, 2017
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Nanomolar affinity protein trans-splicing monitored in real-time by fluorophore–quencher pairs

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Abstract

High background originating from non-reacted, ‘always-on’ fluorescent probes remains a key unsolved problem in life science since washing procedures are not easily applicable. Covalent labeling approaches with simultaneous activation of fluorescence are advantageous to increase sensitivity and to reduce background signal. Here, we combined high-affinity protein trans-splicing with fluorophore/quencher pairs for online detection of covalent N-terminal ‘traceless’ protein labeling under physiological conditions in cellular environments. Substantial fluorescence enhancement at nanomolar probe concentrations was achieved.

Graphical abstract: Nanomolar affinity protein trans-splicing monitored in real-time by fluorophore–quencher pairs

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Publication details

The article was received on 09 Nov 2016, accepted on 06 Dec 2016 and first published on 07 Dec 2016


Article type: Communication
DOI: 10.1039/C6CC08862G
Citation: Chem. Commun., 2017,53, 545-548
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    Nanomolar affinity protein trans-splicing monitored in real-time by fluorophore–quencher pairs

    M. Braner, R. Wieneke and R. Tampé, Chem. Commun., 2017, 53, 545
    DOI: 10.1039/C6CC08862G

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