Protein profiling is a novel and potentially powerful approach for improved diagnosis of various diseases. To this end, peptides and proteins are captured from serum (or other body fluids) and analyzed by mass spectrometry. Pattern analysis of the generated peptide spectra for the presence or absence of specific peaks (biomarkers) allows the classification of individuals, even without identification of the relevant biomarkers themselves.
Glycosylation, however, can significantly influence the safety and efficacy of glycoprotein therapeutics. It plays an important role in maintaining the activity, protease stability and stabilization of quaternary structure. A detailed and accurate monitoring of glycan structures is thus a mandatory task throughout the lifecycle of biotherapeutics.