Recent advancements in nanotechnology provides glycobiologists with an exciting opportunity to more fully explore and exploit the diverse role of glycans in biology. Nanoscale architectures present glycans in scenarios that highly resemblance that seen at the cellular scale. Protein-carbohydrate/glycan interactions are essential to many biological processes. Glycans (mono-, oligo- and poly-saccharides) are the first line of interaction with the extracellular world, with glycan binding proteins (e.g., lectins or toxins) present on one cell (either a eukaryote, prokaryote or virus) interacting with glycan structures present on another opposing cell.1,2 Though these are often low affinity and broad specificity, nature enhances avidity through the use of multivalent glycan and/or lectin displays.3 For example, glycans scaffolded on glycoproteins and/or on patches of glycolipids on the surface of a cell, or multiple copies of lectins and/or lectins with multiple bindings sites displayed at the surface of an opposing cell, provide multivalency that increases the overall binding strength by engaging many individual glycan receptors simultaneously (see Fig. 1). An analogy frequently used to illustrate this concept is the interaction of the two faces of a Velcro™ strip.4 Glycans are inherently complex and lectins are capable of binding a broad range of related carbohydrate structures. As such, binding avidity of ligands to cells surface receptors can be controlled by the number of carbohydrate residues on biomolecular constructs as well as their presentation including branching. Though numerous tools are already available to study and assign protein-glycan interactions, they rely heavily on labeling techniques that can increase heterogeneity and structural complexity. This has hindered many advancements, and as such the development of fast, easy and inexpensive label-free, biosensing tools for the analysis of carbohydrate-protein interactions has become highly desirable.