Site-specific protein labelling and immobilization mediated by microbial transglutaminase

Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjec...

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Veröffentlicht in:	Chemical communications (Cambridge, England) England), 2014-06, Vol.50 (50), p.6604-6606
Hauptverfasser:	Oteng-Pabi, Samuel K, Pardin, Christophe, Stoica, Maria, Keillor, Jeffrey W
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkynes - chemistry Azides - chemistry Catalysis Copper - chemistry Cycloaddition Reaction Enzymes, Immobilized - chemistry Enzymes, Immobilized - metabolism Glutamine - chemistry Glutamine - metabolism Oligopeptides - chemistry Pargyline - analogs & derivatives Pargyline - chemistry Pargyline - metabolism Propylamines - chemistry Propylamines - metabolism Proteins - chemistry Proteins - metabolism Streptomycetaceae - enzymology Substrate Specificity Transglutaminases - metabolism
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Zusammenfassung:	Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjected to copper-assisted azide-alkyne cycloaddition to demonstrate either fluorescent labelling or immobilization.
ISSN:	1359-7345 1364-548X
DOI:	10.1039/c4cc00994k