title: Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces.
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 beta-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human beta1,4-galactosyltransferase-1 and beta1,3-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.
authors.affiliation: Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Germany.
authors.forename: Birgit
authors.initials: B
authors.lastname: Sauerzapfe
authors.forename: Karel
authors.initials: K
authors.lastname: Krenek
authors.forename: Judith
authors.initials: J
authors.lastname: Schmiedel
authors.forename: Warren W
authors.initials: WW
authors.lastname: Wakarchuk
authors.forename: Helena
authors.initials: H
authors.lastname: Pelantová
authors.forename: Vladimir
authors.initials: V
authors.lastname: Kren
authors.forename: Lothar
authors.initials: L
authors.lastname: Elling