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The internalization of antibody via pinocytosis and its pH-dependent interaction with the neonatal Fc receptor (FcRn) play crucial roles in antibody recycling within circulation. To achieve an optimal half-life, the binding of antibodies to FcRn at acidic pH and their release at physiological pH must be carefully characterized. Here, we describe the use of surface plasmon resonance (SPR) to measure the affinity of human IgG1 antibodies to human FcRn in both acidic (pH 6.0) and physiological (pH 7.4) conditions to evaluate the recycling behavior of therapeutic candidates.

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Characterizing pH-Dependent Interactions Between Immunoglobulin and the Neonatal Fc Receptor Using Surface Plasmon Resonance

  • 实验方案

  • 发表日期：

    2026年

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  • Sébastien Menant,
  • Damien Nevoltris,
  • Romain Ollier

摘要

The internalization of antibody via pinocytosis and its pH-dependent interaction with the neonatal Fc receptor (FcRn) play crucial roles in antibody recycling within circulation. To achieve an optimal half-life, the binding of antibodies to FcRn at acidic pH and their release at physiological pH must be carefully characterized. Here, we describe the use of surface plasmon resonance (SPR) to measure the affinity of human IgG1 antibodies to human FcRn in both acidic (pH 6.0) and physiological (pH 7.4) conditions to evaluate the recycling behavior of therapeutic candidates.