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

Sébastien Menant1, Damien Nevoltris2, Romain Ollier2

  • 1AC Immune SA, EPFL Innovation Park, Lausanne, Switzerland. sebastien.menant@acimmune.com.

Methods in Molecular Biology (Clifton, N.J.)
|May 13, 2026
PubMed
Summary

Antibody recycling is vital for drug half-life. This study uses surface plasmon resonance to measure antibody binding to the neonatal Fc receptor (FcRn) at different pH levels, aiding therapeutic development.

Keywords:
AffinityAntibody recyclingIgGNeonatal Fc receptorSPR

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Area of Science:

  • Immunology
  • Pharmacology
  • Biochemistry

Background:

  • Antibody internalization via pinocytosis is essential for circulation.
  • The neonatal Fc receptor (FcRn) mediates pH-dependent antibody binding and recycling.
  • Optimizing antibody half-life requires understanding FcRn interactions at acidic and physiological pH.

Purpose of the Study:

  • To characterize the affinity of human IgG1 antibodies to human FcRn.
  • To evaluate antibody recycling behavior for therapeutic candidates.
  • To assess FcRn binding at acidic (pH 6.0) and physiological (pH 7.4) conditions.

Main Methods:

  • Surface Plasmon Resonance (SPR) was employed for affinity measurements.
  • Human IgG1 antibodies were tested for binding to human FcRn.
  • Binding kinetics were analyzed at two distinct pH values.

Main Results:

  • SPR successfully measured human IgG1 antibody affinity to human FcRn.
  • Affinity differences were observed between acidic and physiological pH conditions.
  • Data provides insights into the pH-dependent FcRn interaction.

Conclusions:

  • SPR is a valuable tool for characterizing antibody-FcRn interactions.
  • Understanding pH-dependent binding is critical for designing therapeutic antibodies with optimal half-lives.
  • This method aids in the evaluation of antibody recycling and therapeutic potential.