ABSTRACT
Antibody (Ab)–antigen (Ag) interactions provide well-defined systems for the analysis of intermolecular interactions between large, complex molecules. The genetic machinery utilized by immunoglobulin genes allows tremendous flexibility in selecting antibodies with specific binding properties. Ab–Ag interactions can be utilized as tools to analyze the binding energetics of a wide range of potential interactions. The molecular species populating the landscape may, however, be different. By developing antibodies to specifically mimic other structures, the diversity of a particular intermolecular interaction landscape can be sampled. In molecular terms, the antibody variable region is a large surface with several potential binding sites. Antibodies have been developed to mimic other structures, both proteins and non-protein molecules. The utilization of antibodies as molecular mimics allows the development of a constrained system of intermolecular interactions where several points in a binding landscape can be analyzed. The strategy utilizes applied molecular evolution in selecting antibody variable regions and utilizing them as probes of an intermolecular interaction landscape.
