Neo-GlycoproteinsCopyright: L. & F. Biomaterialien
The platform of multivalent presentation of glycans is extended by usage of non-glycosylated serum proteins, e.g. bovine serum albumin (BSA). In a two-stage process, functional groups of amino acids side chains (e.g. NH2-) are specifically connected with previously synthesized glycans. The conjugation proceeds under mild conditions in aqueous milieu at room temperature without affecting protein or glycan structure. Analysis of artificial glycosylated proteins (neo-glycoproteins) is achieved by an in-house developed biochemical assay (TNBS Assay) or via gel electrophoresis (S. Böcker et al. (2015)).
The sort and number of conjugated glycan units per protein molecule (modification density) are tunable. Thereby, interaction strength and for certain lectins can be modulated. Neo-glycoproteins are recognized by galectins and bacterial toxins, while the binding strength is raised many times over compared to monovalent ligands due to multivalency effects.