The power of Q-TOF Mass Spectrometric technology has been amply demonstrated for accurate intact mass analysis of biopharmaceuticals and also for the essential task of peptide and protein sequencing. Combined with the earlier development of peptide mapping strategies utilizing specific proteolytic digestion protocols, mass spectrometry is now an essential tool in biopharmaceutical characterisation for manufacturing and regulatory purposes.
Of particular importance is the assignment of co- or post-translational modifications of proteins (PTMs) including Glycosylation, Acylation and Disulfide Bridge configuration. The conjugation of cytotoxic drugs to antibodies to produce ADCs is simply another example of post translational modification of the carrier protein. Here we present how the MS strategies developed for native PTM identification are equally applicable to this exciting field of medical discovery.
