Selected article for: "Fc region and FcRn Neonatal Fc receptor"

Author: Saeed, Abdullah F. U. H.; Wang, Rongzhi; Ling, Sumei; Wang, Shihua
Title: Antibody Engineering for Pursuing a Healthier Future
  • Document date: 2017_3_28
  • ID: 0fegsm1v_107
    Snippet: The Fc region is modulated by engineering the effector function, for example to increase or lessen binding to Fc gamma receptors (FcγRs) or complement factors and the half-life of IgG. The half-life can be extended by improving affinity of Fc for Fc neonatal receptor (FcRn). Moreover, it can be prolonged by engineering pH-dependent antigen binding to enhance recycling of IgG via FcRn, and effective binding to the target molecule. Engineering the.....
    Document: The Fc region is modulated by engineering the effector function, for example to increase or lessen binding to Fc gamma receptors (FcγRs) or complement factors and the half-life of IgG. The half-life can be extended by improving affinity of Fc for Fc neonatal receptor (FcRn). Moreover, it can be prolonged by engineering pH-dependent antigen binding to enhance recycling of IgG via FcRn, and effective binding to the target molecule. Engineering the Fc region permits the development of molecules that are better suited to the pharmacology activity required of them (Vincent and Zurini, 2012; Rath et al., 2015) . Recently, a study investigates engineering the pH-dependent interaction between IgG and FcRn. It involves modulation of constant Fc part of monoclonal human IgG1 (hIgG1) antibodies to improve effector functions and clinical efficacy of next-generation IgG1based therapeutics (Grevys et al., 2015) .

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