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Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies


The rapid growth of the therapeutic antibody market has increased the interest in modeling of the antibody structure and in understanding the factors that affect the function and the stability of antibodies. As of 2006 there were 18 monoclonal antibodies approved for therapeutic use in US, and 14 of them were molecules of the IgG isotype.1 Among these, 50% are humanized IgG1 anti-bodies. The antibody molecule (Figure 1) is formed by two identical heavy chains (~450 residues each) and two identical light chains (~220 residues each).

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