ABSTRACT
Antibody molecules are very amenable to manipulation both chemically and by genetic engineering. As described in Chapter 1, the antibody molecule is made up of a series of domains which are capable of folding into their native structure independently. This has enabled many manipulations of the antibody molecule to be carried out without affecting the conformation of adjacent domains, and allows domains to be moved in position, or substituted with other molecules relatively easily. In addition, the beta sheet structure of the immunoglobulin fold allows some substitutions to be made within domains without loss of activity provided care is taken to ensure the integrity of the domain. In particular, as the antigen binding activity of the V domains is largely conferred by the CDR loops alone, it is possible to make changes in these loops, or switch them from one antibody to another, without disturbing the structure of the framework supporting them. This ease of genetic manipulation has led to the technology of antibody engineering which now allows the specific design of antibody molecules for particular applications.
