NDLI: Detection of transglutaminase activity using click chemistry

Content Provider	Springer Nature Link
Author	Geel, Remon Debets, Marjoke F. Löwik, Dennis W. P. M. Pruijn, Ger J. M. Boelens, Wilbert C.
Copyright Year	2011
Abstract	Transglutaminase 2 (TG2) is a Ca2+-dependent enzyme able to catalyze the formation of ε(γ-glutamyl)-lysine crosslinks between polypeptides, resulting in high molecular mass multimers. We have developed a bioorthogonal chemical method for the labeling of TG2 glutamine-donor proteins. As amine-donor substrates we used a set of azide- and alkyne-containing primary alkylamines that allow, after being crosslinked to glutamine-donor proteins, specific labeling of these proteins via the azide-alkyne cycloaddition. We demonstrate that these azide- and alkyne-functionalized TG2 substrates are cell permeable and suitable for specific labeling of TG2 glutamine-donor substrates in HeLa and Movas cells. Both the Cu(I)-catalyzed and strain promoted azide-alkyne cycloaddition proved applicable for subsequent derivatization of the TG2 substrate proteins with the desired probe. This new method for labeling TG2 substrate proteins introduces flexibility in the detection and/or purification of crosslinked proteins, allowing differential labeling of cellular proteins.
Starting Page	1251
Ending Page	1263
Page Count	13
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	43
Issue Number	3
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2011-12-17
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Transglutaminase Click chemistry Azide Alkyne Cycloaddition Protein modification Life Sciences Analytical Chemistry Biochemistry Proteomics Neurobiology Biochemical Engineering
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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