Chemitope offers a large collection of biotinylated N-linked high-mannose, complex- and hybrid-type glycans along with tumor-associated O-linked glycans to study protein-carbohydrate interactions.
•Our N-linked glycans are functionalized at the anomeric position with a biotin through a β-amide nitrogen recapitulating the natural connectivity between asparagine and glycan.
•Our N-linked glycan-clusters have been designed to evaluate the avidity effect induced by the proximity of several glycans on protein-carbohydrate interactions. The scaffold mimics the relative distance found between glycans within naturally occurring glycan-patches as found at the surface of viral spikes for example.
•Our O-linked glycans are connected to serine or threonine, acetylated at the N-terminal end and separated from the biotin by a PEG linker in order to allow for optimal accessibility once bound to streptavidin.