The glycocalyx is a carbohydrate layer on the cell surface, presenting glycolipids, glycoproteins, proteoglycans and glycosaminoglycans (GAGs). This interface performs important cellular functions including protecting the cell from external pathogenic agents (e.g., toxins and viruses) and mediation of communication between cells. Moreover, the glycocalyx is also the target of diverse glycan binding proteins (lectins). The highly complex diversity and disposition of carbohydrate structures in this layer makes it challenging to study the interactions of the glycocalyx with viruses and lectins. Therefore, several groups have sought to build better-defined models that reproduce selected properties of the glycocalyx, ranging from simple arrays of carbohydrates attached to a surface, to more complex systems in which lipid-linked glycans are presented in fluid layers such as supported lipid bilayers (SLB) or giant unilamellar vesicles (GUVs) that mimic the cell membrane. Several groups have described the synthesis and application of structures mimicking mucin proteins to add a third dimension to their models and increase their similarity to the extracellular matrix. These glycopolymers typically comprise monosaccharides or oligosaccharides attached to a polymer backbone, an anchor at one end (e.g., a lipid or covalent bond to a surface) and sometimes a fluorophore at the other end or along the chain. They have been incorporated, for example, into supported lipid bilayers (SLB) and arrays to study binding with Influenza A viruses, and introduced onto red blood cell membranes to study interactions with Concanavalin A and Sambucus nigra agglutinin.