. . . "Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectinmediated 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 \u03B2-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human \u03B21,4-galactosyl-transferase-1 and \u03B21,3-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" . . "306923" . . . "Sauerzapfe, B." . "Glycoconjugate Journal" . "chemo-enzymatic sysnthesis; galectin binding; biomaterials"@en . "P(IAA400200503), P(LC06010), Z(AV0Z50200510)" . "Pelantov\u00E1, Helena" . . "7"^^ . "2" . . "K\u0159enek, Karel" . "Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces"@en . "Elling, L." . . "Wakarchuk, W. W." . "000263417500003" . . . . "3"^^ . . "Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectinmediated 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 \u03B2-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human \u03B21,4-galactosyl-transferase-1 and \u03B21,3-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"@en . "26" . "Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces" . . "Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces" . . "18"^^ . . . . . "K\u0159en, Vladim\u00EDr" . "RIV/61388971:_____/09:00327089!RIV10-MSM-61388971" . "RIV/61388971:_____/09:00327089" . "Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces"@en . . "0282-0080" . "[6C3837874424]" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . "Schmiedel, J." .