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LFBD192 is a modified monomeric recombinant human IgG1 Fc fragment engineered for the dual targeting of the neonatal Fc receptor (FcRn) and activating Fc gamma receptors (FcγRs). Developed by LFB Biotechnologies, the molecule incorporates six specific mutations (Y296W, K334N, P352S, A378V, V397M, and N434Y) that significantly enhance its binding affinity for FcRn at acidic pH and for various FcγRs (including FcγRI, FcγRIIa, and FcγRIIIa) at physiological pH. This dual mechanism of action allows LFBD192 to accelerate the clearance of pathogenic endogenous IgG antibodies by saturating FcRn while simultaneously blocking the activation of effector cells by immune complexes through FcγR inhibition. Unlike multimeric Fc constructs, LFBD192's monomeric structure is designed to minimize the risk of FcγR cross-linking and subsequent cytokine release syndrome. It is primarily being investigated for the treatment of IgG-dependent autoimmune pathologies, including immune thrombocytopenia (ITP) and rheumatoid arthritis.
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