| DOI | Resolve DOI: https://doi.org/10.1007/s10719-008-9172-2 |
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| Author | Search for: Sauerzapfe, Birgit; Search for: Krenek, Karel; Search for: Schmiedel, Judith; Search for: Wakarchuk, Warren W.1; Search for: Pelantová, Helena; Search for: Kren, Vladimir; Search for: Elling, Lothar |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Subject | poly-LacNAc; chemo-enzymatic synthesis; galectin binding; ECM glycoproteins; biomaterials |
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| Abstract | Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectin-mediated cell adhesion to extra-cellular matrix (ECM) proteins. We here present the biofunctionalization of surfaces with poly-LacNAc structures and subsequent binding of ECM glycoproteins. First, we synthesized β-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human β1,4-galactosyltransferase-1 and β1,3-N-acetylglucosaminyltransferase from Helicobacter pylori. These compounds were also used for kinetic characterization of glycosyltransferases and lectin binding assays. A mixture of poly-LacNAc-structures covalently coupled to functionalized microtiter plates were identified for best binding to our model galectin His6CGL2. We further demonstrate for the first time that these poly-LacNAc surfaces are suitable for further galectin-mediated binding of the ECM glycoproteins laminin and fibronectin. This new technology should facilitate cell adhesion to biofunctionalized surfaces by imitating the natural ECM microenvironment. |
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| Publication date | 2008-09-28 |
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| Publisher | Springer |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 9381535 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 537b7179-0fb6-48d3-ac48-3d42582300ab |
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| Record created | 2009-07-10 |
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| Record modified | 2020-04-15 |
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