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<p>Human (<i>h</i>)IgG2 monoclonal antibodies (mAbs) are potent agonists due, in part, to their ability to undergo disulfide shuffling within their hinge regions. Herein, we describe a rapid, sensitive, collision-induced unfolding (CIU) assay that possesses a predictive relationship between gas-phase protein unfolding and agonism in <i>h</i>IgG2 variants. Furthermore, our results highlight the significance of hinge engineering in tuning mAb structure-function relationships for the development of future biotherapeutics.</p>

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Gas-phase unfolding assay rapidly predicts structure-function relationships in engineered antibodies with tuned flexibilities

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月29日

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  • Rosendo C. Villafuerte-Vega,
  • Michael R. Armbruster,
  • Hayden Fisher,
  • Isabel G. Elliott,
  • H. T. Claude Chan,
  • Tatyana Inzhelevskaya,
  • C. Ian Mockridge,
  • Christine A. Penfold,
  • Patrick J. Duriez,
  • Mark S. Cragg,
  • Brandon T. Ruotolo

摘要

Human (h)IgG2 monoclonal antibodies (mAbs) are potent agonists due, in part, to their ability to undergo disulfide shuffling within their hinge regions. Herein, we describe a rapid, sensitive, collision-induced unfolding (CIU) assay that possesses a predictive relationship between gas-phase protein unfolding and agonism in hIgG2 variants. Furthermore, our results highlight the significance of hinge engineering in tuning mAb structure-function relationships for the development of future biotherapeutics.