Date: December 9, 2021
Time: 6:00am (PST), 9:00am (EST)
As the number of biotherapeutic candidates in development is increasing, the requirements of analytical tools to understand the molecules better early in the process are rising, simultaneously. To understand product quality attributes (PQAs) fully, identification, localization, and relative quantification are key. Mass spectrometry (MS) plays an important role with peptide mapping being the gold standard to assess post-translational modifications (PTM). However, traditionally used collision-induced dissociation (CID) has a number of limitations in PTM identification and localization. Here, the novel fragmentation technique electron activated dissociation (EAD) was employed for peptide mapping of a multispecific monoclonal antibody (mAb) as well as IgG1 and IgG4 mAb samples. The samples were denatured, reduced and enzymatically digested prior to injection onto a novel Q-TOF instrument (ZenoTOF 7600 system, SCIEX) with data-dependent acquisition with either CID or EAD mode. A specific focus was put on assessing challenging PTMs, such as glycosylations, amino acid isomers and the localization of a sulfation on a singly charged peptide.
- Recognize the characterization of challenging PTMs such as glycosylations and amino acid isomers
- Discuss the fragments providing positioning information that could be detected with EAD
- Discover how you can characterize biotherapeutics with the novel ZenoTOF 7600 system
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