Multivalency is a fundamental principle in nature that leads to high-affinity intermolecular recognition through multiple cooperative interactions that overcome the weak individual binding of constituents. For example, multivalency plays a critical role in protein-carbohydrate interactions that participate in many essential biological processes. The design of high-affinity multivalent glycoconjugates that engage saccharide-binding proteins results in systems capable of interfering with these biological processes and holds promise for therapeutic design and bioengineering applications. Leveraging subcomponent self-assembly, a versatile and tunable synthetic platform for the synthesis of metallosupramolecular glycoassemblies is presented. This approach enables precise control over molecular parameters such as size, shape, charge, surface density, and valency. A diverse family of well-defined, multivalent glycoassemblies prepared through purposeful modifications to ligand design will be presented. Evaluation of these complexes as multivalent binders to protein targets demonstrates the optimal saccharide topology and architectural parameters that lead to high affinity interactions, revealing insights into the impact of rational synthetic design on molecular recognition strength. The presented studies lead to an enhanced understanding of structure-function relationships governing protein-saccharide interactions at the molecular level and guide a systematic approach towards optimizing glyconanoassembly binding parameters.