Assessment of quality attributes of biotherapeutics leveraging a novel fragmentation technique

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.