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A biparatopic antibody (BpAb) is a bispecific antibody that recognizes two different epitopes of the same antigen. Many BpAbs have been developed to control the structures of immunocomplexes different from that with the original antibodies. Various binding modes are enabled, including the cross-linking pattern of binding and 1:1-binding, which influence the biological activities of BpAbs. In this chapter, we describe the analytical methods for characterizing cross-linking activities. Taking a development campaign for bivalent asymmetric BpAbs targeting TNFR2 as an example, combined analysis is described using size-exclusion chromatography–multi-angle light scattering, mass photometry, and surface plasmon resonance.

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Multimodal Physicochemical Characterization of Cross-Linking Activities of Biparatopic Antibodies

  • 实验方案

  • 发表日期：

    2026年

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  • Hiroki Akiba,
  • Kohei Shiba,
  • Kouhei Tsumoto,
  • Hiroaki Ohno,
  • Haruhiko Kamada

摘要

A biparatopic antibody (BpAb) is a bispecific antibody that recognizes two different epitopes of the same antigen. Many BpAbs have been developed to control the structures of immunocomplexes different from that with the original antibodies. Various binding modes are enabled, including the cross-linking pattern of binding and 1:1-binding, which influence the biological activities of BpAbs. In this chapter, we describe the analytical methods for characterizing cross-linking activities. Taking a development campaign for bivalent asymmetric BpAbs targeting TNFR2 as an example, combined analysis is described using size-exclusion chromatography–multi-angle light scattering, mass photometry, and surface plasmon resonance.