Glycan analysis of monoclonal antibodies

The aim of this thesis is to develop a sample treatment and analysis method for glycan analysis of trastuzumab which is used as a therapeutic monoclonal antibody during treatment of breast cancer. Correct glycan structure of monoclonal antibody is essential for functional and biological activity of the related monoclonal antibody such as identification of antigens triggered by immune system cells, regulation of the signaling activities and physicochemical properties of produced therapeutics. For these reasons, rapid and accurate monitoring of glycan structure is very critical for therapeutic drug production, biosimilar drug production and their quality control processes. The N-glycan structure of trastuzumab was analysed by MALDI-TOF-MS system using a number of enymatic reactions and solid phase extraction techniques. A qualitative analysis of N-glycan structures obtained by a special software program. N-Glycans of trastuzumab named G0-GlcNAc, G0F-GlcNAc, G0, G0F, G1F (according to CFG notation) are detected with MALDI-QIT-TOF-MS by mass/charge ratios and find out a rapid and throughput analysis method. Keywords: Monoclonal antibody, MALDI-TOF-MS, N-glycan, trastuzumab.