Immunoglobulin G Fc engineering for localized therapy: Eliminating neonatal Fc receptor interactions and ensuring purification using protein A.

ABSTRACT: Monoclonal antibodies (mAbs) and bispecific antibodies (bsAbs) have transformed therapeutic strategies for various diseases. However, administering them can lead to unwanted adverse effects and insufficient delivery to local disease sites. Recent research has shown that substitutions in the immunoglobulin G (IgG) Fc region, designed to eliminate binding to the neonatal Fc receptor (FcRn), which accelerates clearance from systemic circulation, may improve the safety of antibody therapies intended for localized use. A major concern with these substitutions is their ability to impair binding to protein A, which is considered the gold standard for large-scale antibody purification. In this study, we investigated multiple amino acid substitutions at residues I253, H310, H435, and Y436-positions

SUBMITTER: Kato A 

PROVIDER: S-EPMC12542301 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature