Carbohydrate−protein interactions play key roles in a wide variety of biological processes. These interactions are usually weak, with dissociation constants in the low millimolar to high micromolar range. Nature uses multivalency to reach high avidities via the glycoside cluster effect. Capitalizing on this effect, numerous synthetic multivalent glycoconjugates have been described and used as ligands for carbohydrate-binding proteins. However, valency is only one of the several parameters governing the binding mechanisms that are different for every biological receptor, making it almost impossible to predict. In this context, ligand optimization requires the screening of a large number of structures with different valencies, rigidities/ flexibilities, and architectures. In this article, we describe a screening platform based on a glycodendrimer array and its use to determine the key parameters for high-affinity ligands of lectin. Several glycoclusters and glycodendrimers displaying varying numbers of α-N-acetylgalactosamine residues were covalently attached on glass slides, and their bindings were studied with the fluorophore-functionalized Helix pomatia agglutinin (HPA) used as a lectin model. This technique requires minimal quantities of glycoconjugate compared to those for other techniques and affords useful information on the binding strength. Building of the glycodendrimer array and quantification of the interactions with HPA are described.