Antigens are proteins produced by the immune system to detect and act upon any foreign objects (antigens). Their high affinity and specificity makes lab-produced monoclonal antibodies (mAbs) attractive as potential drugs. In the last three decades the global market for therapeutic mAbs has been growing exponentially.
The binding properties of a typical antibody are primarily determined by the structure of just six hypervariable loops called Complementarity Determining Regions or CDRs. In my DPhil I study the structural and chemical properties of CDRs and how they relate to the binding properties of an antibody, with the ultimate goal of being able to design a functional antibody for a novel target from the available structural and sequential CDR repertoire.