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http://hdl.handle.net/1942/16388
Title: | Sortase A‐mediated protein ligation for site‐specific ‘click’ functionalization and oriented coupling of nanobodies to biosensor material surfaces or contrast probes | Authors: | TA, Duy Tien STEEN REDEKER, Erik GUEDENS, Wanda ADRIAENSENS, Peter |
Issue Date: | 2014 | Source: | 12th Chemistry Conference for Young Scientists, Blankenberge, 27-29/02/2014 | Abstract: | Specificity, sensitivity and reproducibility are critical issues to be improved regarding a homogeneously oriented protein coupling to surfaces for the development of next generation functional bio-materials such as biosensors. In the present study, we describe the development of a robust enzymatic strategy to accomplish all these requirements using the recombinant sortase A. This transpeptidase, derived from the bacterium Staphylococcus aureus, recognizes the conserved LPETG motif in a protein sequence and catalyzes the transpeptidation of an oligoglycine to this protein target. Particularly, the LPETG motif is engineered at the C-terminal region of the variable domain of the single-domain heavy chain antibody (or nanobody) targeting the Vascular Cell Adhesion Molecule 1 (VCAM1). The sortase A-catalyzed transpeptidation is subsequently performed to ligate the engineered nanobodies to various oligoglycine-containing co-substrates including labeling molecules, ‘clickable’ functionalities for further ‘click’ chemistry-mediated coupling, or material surfaces. | Keywords: | nanobody; sortase A; surface coupling; VCAM1 | Document URI: | http://hdl.handle.net/1942/16388 | Category: | C2 | Type: | Conference Material |
Appears in Collections: | Research publications |
Files in This Item:
File | Description | Size | Format | |
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Abstract_Tien_KVCV-final.pdf | Conference material | 644.26 kB | Adobe PDF | View/Open |
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