Sortase-mediated ligation of purely artificial building blocks
Congratulations to Tayebeh on her recent publication!
The collaboration between the Schwaneberg and Böker groups resulted in the publication of a novel application of sortase A. Sortase A, an enzyme produced by Staphylococcus aureus, has long been studied as a catalyst for the ligation of proteins with various biomolecules, particles and surfaces. The present work shows an enzymatically catalyzed linkage of two synthetic blocks. First, the linkage between silica nanoparticles with polymer and between silica nanoparticles of different size by sortase A catalysis was investigated. Second, the linkage between two commercially available polymers by sortase A via MALDI-TOF-MS was proved. For this purpose, the building blocks were first equipped with the recognition sequence needed for sortase A reaction—the conserved peptide LPETG—and a pentaglycine motif. The linkage of the peptides to the nanoparticle surfaces and polymer functional end groups were performed by thiol click reaction between cysteine residues of the peptide motifs and C=C-decorated building blocks. These findings suggest a new ligation method for synthetic species.
Part of this work was performed at the Center for Chemical Polymer Technology in DWI, which was supported by the EU and the federal state of North Rhine–Westphalia.
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Dai, X., Mate, D. M., Glebe, U., Mirzaei, Garakani, T., Körner, A., Schwaneberg, U., Böker, A.; Sortase-Mediated Ligation of Purely Artificial Building Blocks, Polymers, 2018, 10, 151; doi:10.3390/polym10020151