The Power of Many? Evaluating the Impact of Avidity on Tumor Targeting

Our goal is to evaluate how constructs with the same apparent binding strength interact differently with cells and tumors and harness these differences to improve therapeutic delivery. We engineered a library of fusion proteins with two variations of a human epidermal growth factor receptor 2 (HER2) targeting moiety – one with high affinity and one with low affinity. By altering the valency of the binding moieties on our fusion protein, we create a construct containing the weak binder at a high valency that possesses the same apparent dissociation constant (KD) as a construct containing the strong binder at a lower valency.