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Please use this identifier to cite or link to this item: 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
Issue Date: 2014
Citation: 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.
URI: http://hdl.handle.net/1942/16388
Category: C2
Type: Conference Material
Appears in Collections: Research publications

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