Water-soluble, substrate for sortase mediated labeling of proteins. Sortase catalyzes a transpeptidase reaction between a specific internal sequence of a protein and an amine group present on the N-terminus of triglycine recently has become an area of great interest. This method of labeling proteins has been denoted as “Sortagging”.
Proteins conjugated to DBCO-Gly-Gly-Gly can be further modified with azide-containing molecules creating site-specific protein conjugates. Examples of creating protein conjugates using sortagging include site-specifically PEGylating proteins,1 site-specific protein-lipid conjugates,2 and constructing peptides and glycosylphosphatidylinositol chimeras.3 Sortase has also been used in peptide synthesis to cyclize peptides to create macrocyclic peptides, glycopeptides4 and protein−protein conjugates.5
- Dougan, S. K., et al. (2011). Sortase-catalyzed transformations that improve the properties of cytokines. Proc Natl Acad Sci U S A, 108 (8), 3169-74. [PubMed]
- Miller, G. M., et al. (2008). Lipid modification of proteins through sortase-catalyzed transpeptidation. J Am Chem Soc., 130 (48), 16338-43. [PubMed]
- Swarts, B. M., et al. (2009). Sortase-catalyzed peptide-glycosylphosphatidylinositol analogue ligation. J Am Chem Soc., 131 (29), 9878-9. [PubMed]
- Wu, Z., et al. (2011). Sortase A-catalyzed peptide cyclization for the synthesis of macrocyclic peptides and glycopeptides . Chem Commun (Camb)., 47 (32), 9218-20. [PubMed]
- Dougan, S. K., et al. (2012). Preparation of unnatural N-to-N and C-to-C protein fusions. Proc Natl Acad Sci U S A, 109 (30), 11993-8. [PubMed]
Heterobifunctional reagent activated with terminal alkyne group and methyltetrazine moiety.