Glycopolymers offer many opportunities for interfacing synthetic materials with biological systems. However, the nature of the interactions between glycopolymers and their biological targets, lectins, and the structural features necessary to obtain high-affinity materials are not fully understood. Here, the enhancement in binding affinity of multivalent glycopolymers to their corresponding lectins is investigated by quartz-crystal microbalance with dissipation monitoring (QCM-d). This technique allows the conformation of the adsorbed polymers to be probed and the direct observation of spanning of multiple binding sites on lectin-functional surfaces. The measured affinity was compared to the anti-adhesion activity of the polymers in solution, and it is shown that increased association constants did not directly correlate with inhibitory activity.