The analysis of the aggregation phenomenon of therapeutic proteins is of crucial importance as more and more pharmaceutical products are proteins or peptides. Aggregation can not only result in reduced efficacy of biopharmaceuticals, but also increases the risk of inducing an immune response to the mAb rather than the pathogenic antigen it was supposed to detect. CovalX offers a unique technique for the direct characterization of therapeutic protein samples based on High-Mass MALDI mass spectrometry. This technique is often utilized orthagonally to SEC, SEC-MALS or AUC when a discrete measurement of the aggregates is desired. The mass measurement provides a direct detection of the species present, not an average as many techniques.
High-Mass MALDI TOF analysis (CovalX HM1) of aggregated sample of the therapeutic protein Hab41 before (black) and after (red) cross-linking. The sample has been submitted to SEC before cross-linking protocol with K200 MALDI MS Stabilization Kit.
The fraction analyzed exhibit a dimer (350 kDa). The high-mass analysis allow to distinguish between covalent and non covalent aggregation.
High Mass MALDI ToF analysis of an aggregated sample of therapeutic protein Hab42 before (black) and after (red) cross-linking. The sample has been submitted to SEC before cross-linking protocol using K200 MALDI MS stabilization kit. The fraction analyzed exhibits a dimer (303 kDa) and hexamer (910 kDa).
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