ArticleCommunications chemistry2025
High-throughput glycosylation screening method for biologics development using MALDI-TOF-MS.
Article in Communications chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Comparative evaluation of different MALDI-TOF-MS platforms for plasma IgG N-glycan profiling: impact on analytical performance and clinical conclusions.Analytical and bioanalytical chemistry · 2026Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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
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Registered trials
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