Host cell proteins (HCPs) are major impurities generated by the host organism and generally present at the trace level in purified final biopharmaceutical products. These impurities can have detrimental effects on quality, safety and efficacy of drug product. And HCPs can sometimes trigger an unpredictable immunogenic response.

Protein glycosylation is one of the most important quality attributes related to the development of protein therapeutics including antibody or Fc-fusion protein therapeutics. Especially, changes in the efficacy or toxicity of a protein therapeutics can occur as a result of changes in pharmacokinetics, pharmacodynamics or immunogenicity depending on the nature and extent of protein glycosylation. Therefore, Both of glycosylation and impurity analysis of monoclonal antibody products are important for quality control.

In this research, using Nano flow liquid chromatography tandem mass spectrometry (LC–MS/MS)methods trace-level HCPs and intact glycopeptides of monoclonal antibody drug products were simultaneously quantified from same raw data. From original monoclonal antibody product, four HCPs were quantified less than 5ppm and over forty intact glycopeptide were simultaneously quantified. Monoclonal antibody products under processing purification optimization were more number of HCPs and less number of intact glycopeptides quantified than original product. This simultaneously quantified method of impurities (Trace Host Cell Proteins) and intact glyopeptides can be applied to any drug product routine quality control analysis.