Cell therapy products emerge from a long process of cell culture, differentiation and purification steps where appropriate cell identity and purity monitoring are mandatory. The characterization of human MSCs used for manufacturing of cell therapy products requires the development and the validation of analytical methods to encounter biopharmaceutical requirements.

Monoclonal antibodies are among the most promising molecules for the pharmaceutical industry, but their characterization remains very challenging due to their complexity. Although mass spectrometry is now a well established technique for development work,some people are still reluctant to use it for batch release, as it is believed to be expensive and time consuming. In the present work, we present peptide mapping methodologies that can be easily used to characterize monoclonal antibodies. Tryptic peptides are usually separated by reversed-phase chromatography before UV and/or MS detection. We show that HILIC mode (Hydrophilic Interaction Liquid Chromatography) can be an interesting alternative, especially for an effi cient separation of glycopeptides.

Biopharmaceuticals are known to have a greater potential for inducing immune response than conventional small molecule drugs. As a significant safety and efficacy problem, immunogenicity is a major concern for regulatory agencies. Immunogenicity is usually evaluated through the detection and characterization of treatment-induced anti-drug antibodies (ADAs).

Monoclonal antibodies are among the most promising molecules for the pharmaceutical industry, but their characterization remains very challenging due to their complexity.