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Issue 46, 2016
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Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation

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Abstract

Protein glutathionylation is one of the major cysteine oxidative modifications in response to reactive oxygen species (ROS). We recently developed a clickable glutathione approach for detecting glutathionylation by using a glutathione synthetase mutant (GS M4) that synthesizes azido-glutathione (γGlu-Cys-azido-Ala) in situ in cells. In order to demonstrate the versatility of clickable glutathione and to increase the chemical tools for detecting glutathionylation, we sought to develop clickable glutathione that uses tetrazine-alkene bioorthogonal chemistry. Here we report two alkene-containing glycine surrogates (allyl-Gly and allyl-Ser) for the biosynthesis of clickable glutathione and their use for detection, enrichment, and identification of glutathionylated proteins. Our results provide chemical tools (allyl-Gly and allyl-Ser for GS M4) for versatile characterization of protein glutathionylation. In addition, we show that the active site of GS can be tuned to introduce a small size chemical tag on glutathione for exploring glutathione function in cells.

Graphical abstract: Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation

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Publication details

The article was received on 19 Sep 2016, accepted on 28 Oct 2016 and first published on 28 Oct 2016


Article type: Paper
DOI: 10.1039/C6OB02050J
Citation: Org. Biomol. Chem., 2016,14, 10886-10893
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    Clickable glutathione using tetrazine-alkene bioorthogonal chemistry for detecting protein glutathionylation

    D. N. Kekulandara, K. T. G. Samarasinghe, D. N. P. Munkanatta Godage and Y. Ahn, Org. Biomol. Chem., 2016, 14, 10886
    DOI: 10.1039/C6OB02050J

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