Analysis Biomolecular Interactions of Monoclonal Antibodies with Nonspecifically with Polyclonal Antibodies by BLI (CAT#: STEM-MB-0128-CJ)

Introduction

There are a daunting number of factors that influence the effectiveness and success of therapeutic mAbs. The most important issues relate to the specific biological pathways being targeted. For example, the optimal binding affinity and antigen epitope (mediated by the antibody variable domains) as well as the optimal type and level of effector function (mediated by the antibody constant domains) are dependent on the specific therapeutic target. The pharmacokinetics and biodistribution of therapeutic mAbs, which are influenced by the target antigen and recycling Fc receptors, also significantly impact their effectiveness.

The same variable and constant regions of mAbs that mediate affinity interactions can also participate in nonaffinity interactions with either themselves (selfinteractions) or with other molecules (polyspecific interactions). The potential negative ramifications of these colloidal interactions are significant and are also important determinants of the success of therapeutic mAbs. Attractive self-interactions between antibodies (either in their native or non-native conformations) can lead to aggregation, abnormally high viscosity, liquid–liquid phase separation, and opalescence. Polyspecific antibody interactions are also concerning because they can lead to off-target effects as well as fast antibody clearance.