Article

Computational design of monomeric Fc variants with distinct pH-responsive FcRn-binding profiles

2025-05-29

Abstract excerpt

IgG1 and IgG4 antibodies form a ∼150 kDa homodimer through dimerization of the Fc domain, which prolongs their in vivo half-life via pH-dependent binding to the neonatal Fc receptor (FcRn). Conformationally stable, half-life-extended monomeric Fc (mFc) variants offer a promising platform for antibodies and Fc-fusion therapeutics, enabling deeper tissue penetration, reduced toxicity, and simplified manufacturing....

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Literature Corpus work: e8d9ef32-4577-5f3c-9677-d5fbf61bc674
DOI: 10.1101/2025.05.26.656075

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