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<p>Cetuximab and Tocilizumab are significant therapeutic monoclonal antibodies used in the treatment of head and neck malignancies and severe COVID-19 pneumonia, respectively. Given their potential interaction with peanut lectin, patients receiving these therapies should avoid consuming peanuts. In this study, we present a comprehensive multimodal approach using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), high-resolution mass spectrometry (Q-IMS-TOF MS), and size exclusion chromatography to investigate the interactions between these antibodies and lectin derived from peanuts. The role of glycan structures in mediating these interactions was analyzed. For Cetuximab, the glycans identified included G0F, G1FN, G2F, G0, G1, G2, G0N, G1N, M5, and M6. Among these, G1, G2, and M6 were not involved in binding with peanut lectin. In Tocilizumab, the glycans G0F, G1F1, G1FN, G0, G1, G2, G0N, G1N, M5, and M6 were detected, but only G0F, G1F1, and G0 participated in lectin interaction. This detailed glycan analysis provides valuable insights into the specific glycan-mediated binding mechanisms between monoclonal antibodies and lectins, which may inform future therapeutic strategies and dietary considerations for patients undergoing antibody treatments. </p> Graphical abstract <p></p>

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Monitoring interaction between Cetuximab and Tocilizumab with peanut agglutinin lectin

  • 期刊论文

  • 发表日期：

    2025年7月8日

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  • Negar Saeedi,
  • Mohammad Ali As’habi,
  • Amirreza Sharif,
  • Sepideh Parsapour,
  • Elham Habibi,
  • Hassan Y. Aboul-Enein,
  • Alireza Ghassempour

摘要

Cetuximab and Tocilizumab are significant therapeutic monoclonal antibodies used in the treatment of head and neck malignancies and severe COVID-19 pneumonia, respectively. Given their potential interaction with peanut lectin, patients receiving these therapies should avoid consuming peanuts. In this study, we present a comprehensive multimodal approach using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), high-resolution mass spectrometry (Q-IMS-TOF MS), and size exclusion chromatography to investigate the interactions between these antibodies and lectin derived from peanuts. The role of glycan structures in mediating these interactions was analyzed. For Cetuximab, the glycans identified included G0F, G1FN, G2F, G0, G1, G2, G0N, G1N, M5, and M6. Among these, G1, G2, and M6 were not involved in binding with peanut lectin. In Tocilizumab, the glycans G0F, G1F1, G1FN, G0, G1, G2, G0N, G1N, M5, and M6 were detected, but only G0F, G1F1, and G0 participated in lectin interaction. This detailed glycan analysis provides valuable insights into the specific glycan-mediated binding mechanisms between monoclonal antibodies and lectins, which may inform future therapeutic strategies and dietary considerations for patients undergoing antibody treatments.

Graphical abstract