Monovalent IgG4 molecules: immunoglobulin Fc mutations that result in a monomeric structure.

ABSTRACT: Antibodies have become the fastest growing class of biological therapeutics, in part due to their exquisite specificity and ability to modulate protein-protein interactions with a high biological potency. The relatively large size and bivalency of antibodies, however, limits their use as therapeutics in certain circumstances. Antibody fragments, such as single-chain variable fragments and antigen binding-fragments, have emerged as viable alternatives, but without further modifications these monovalent formats have reduced terminal serum half-lives because of their small size and lack of an Fc domain, which is required for FcRn-mediated recycling. Using rational engineering of the IgG4 Fc domain to disrupt key interactions at the CH3-CH3 interface, we identified a number of point mutations

SUBMITTER: Wilkinson IC 

PROVIDER: S-EPMC4169034 | biostudies-literature | 2013 May-Jun

REPOSITORIES: biostudies-literature