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<p>Glycosylation is a critical quality attribute of therapeutic proteins, yet current analytical methods often fail to meet rapid, high-throughput demands. Here, we adopted an optimized glycosylation analysis method for the quality control of therapeutic proteins that combines the speed of MALDI-TOF-MS with the precision of a full glycome internal-standard approach. With 96-well-plate compatibility, the method enables the analysis of at least 192 samples in a single experiment and offers a highly promising solution for biopharmaceutical quality-control scenarios that demand both speed and high throughput capabilities. The suitability of the method was validated on trastuzumab (Herceptin®) with high precision (CV ~ 10%) and broad linearity (R<sup>2</sup> &gt; 0.99) as well as fusion proteins (EPO) with multiple glycosylation sites and complex glycan structures. Excellent linearity, repeatability, and stability were demonstrated in the qualification study. The method offers significant benefits for characterizing N-glycans in glycosylated biologics, with applications ranging from early clone selection to batch-to-batch consistency control, as well as comparative assessments between biosimilars and reference drugs.</p>

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High-throughput glycosylation screening method for biologics development using MALDI-TOF-MS

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年10月2日

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  • Weilong Zhang,
  • Liqi Xie,
  • Huijuan Zhao,
  • Xiaonan Ma,
  • Shifang Ren

摘要

Glycosylation is a critical quality attribute of therapeutic proteins, yet current analytical methods often fail to meet rapid, high-throughput demands. Here, we adopted an optimized glycosylation analysis method for the quality control of therapeutic proteins that combines the speed of MALDI-TOF-MS with the precision of a full glycome internal-standard approach. With 96-well-plate compatibility, the method enables the analysis of at least 192 samples in a single experiment and offers a highly promising solution for biopharmaceutical quality-control scenarios that demand both speed and high throughput capabilities. The suitability of the method was validated on trastuzumab (Herceptin®) with high precision (CV ~ 10%) and broad linearity (R2 > 0.99) as well as fusion proteins (EPO) with multiple glycosylation sites and complex glycan structures. Excellent linearity, repeatability, and stability were demonstrated in the qualification study. The method offers significant benefits for characterizing N-glycans in glycosylated biologics, with applications ranging from early clone selection to batch-to-batch consistency control, as well as comparative assessments between biosimilars and reference drugs.