期刊
GLYCOCONJUGATE JOURNAL
卷 26, 期 2, 页码 141-159出版社
SPRINGER
DOI: 10.1007/s10719-008-9172-2
关键词
Poly-LacNAc; Chemo-enzymatic synthesis; Galectin binding; ECM glycoproteins; Biomaterials
资金
- DFG Research Training Group 1035 Biointerface
- DAAD-AV CR [PPP-D7-CZ26/04-05D/03/44448]
- Boehringer Ingelheim Foundation Travel Allowances
- [MSMT LC06010]
- [GAAVCR IAA400200503]
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 beta-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human beta 1,4-galactosyltransferase-1 and beta 1,3-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 His(6)CGL2. 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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