Their diversity (idiotypic variation) represents the central aspect of the humoral immune response. Antigen binding sites are formed by the interaction of hypervariable loop regions exposed near the N-terminus of the polypeptide chains - the complementary determining regions (CDRs), which are surrounded by relatively invariant framework residues. The individual chains are globular domains that are highly conserved between different immunoglobulins (constant region) or contain sequence variability (variable region). Form Follows Function: Domain Structure of an IgG Antibody 1 They are bifunctional molecules with a basic symmetrical structure consisting of pairs of identical heavy and light chains linked through disulfide bridges (Figure 1). Improvements are due in all areas of the pharmaceutical supply chain but especially in downstream processing to manage current manufacturing challenges and are therefore vital for the long-term success of the sector.Īntibodies represent a class of flexible molecular adaptors that play a vital role in the adaptive immune systems of vertebrates.
While the commercialization of MAbs is gathering momentum, the sector is facing a worldwide shortfall of available biomanufacturing capacity that is becoming a critical strategic limitation, especially for companies without established market access.
Even with conservative assumptions about growing attrition rates, substitution pressure, and margin squeezes, MAb sales will probably reach a stable plateau of $20 billion by 2010. Monoclonal antibodies (MAbs) represent the fastest growing pharmaceutical market segment.
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