Abstract
Monoclonal antibodies (mAbs) typically consist of two light and heavy chains with ~25 and ~50kDa molecular weigt. The mAb primary structure is of utmost importance as it accounts for the physicochemical properties of the antibody and therefore is responsible for efficacy and possible unwanted side effects of biologics. The correct amino acid sequence is commonly determined by the so-called peptide mapping (PM) approach. For PM the mAb is enzymatically cleaved into different peptides, which are subsequently analyzed by liquid chromatography online coupled to mass spectrometry (MS). By this, the correct amino acid sequence can be unambiguously determined. Furthermore, PM is widely used for site-specific analysis of posttranslational and cotranslational modifications of amino acid side chains. This powerful technology therefore is widely used in the biopharmaceutical industry for testing as well as for extended characterization and comparability analysis during drug candidate development. Finally, MS is currently more often used as so-called multiattribute method as an overall control strategy including characterization as well as release testing of biopharmaceutical development candidates.
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