Glycosylation of proteins is the most common post-translational modification in eukaryotes. To understand the role of glycoconjugates in cellular processes, structure analysis of them is required.
Glycoproteomics is a subdicipline of proteomics covering glycosylation analysis of glycoconjugates. Using high-throughput mass spectrometers, glycosylation analysis have been achieved for years.
Glycomics is an important discipline covering glycan structure analysis of a given glycome. Thanks to glycomics, we learn the role of glycans in cellular pathways.
Mass spectrometry based glyco-analytical methods provide great opportunity to chracterize glycan structures of biomolecules such as glycoproteins and protein biopharmaceuticals.
Also, clinical glycomics is an important study, allowing to investigate alteration of glycans in disease and normal situations.
Monoclonal antibodies (mAbs) are protein biopharmaceuticals that are used for the treatment of various diseases such as cancer.
Monitoring PTM’s, especially glycan diversity at each site, is crucial for the development process of mAbs. Thus, analysis of mAbs by reliable analytic approaches is needed.
We analyze mAbs using MALDI-MS, LC-MS/MS, HPLC-Fld and CE-MS at three level:
Besides them, we perform sequence confirmation of mAbs by mass spectrometry.
Bioanalytical Method Development
Efficient analysis of glycopeptides and glycans by MS is crucial. In order to enhance analysis efficiency of glycopeptides and glycans, enrichment or purification step is required. We develop bioanalytical methods for the fast and efficient analysis of glycoconjugates, which include various solid-phase extraction platforms.
Proteomics is a field that identifies protein structure and function. The term “proteome” refers to the whole proteins in a tissue or a cell produced by an organism.
Quantification of proteins in a sample is a challenging task. As an emerging area, quantitative proteomics have become an important analytical approach to detect the amount of proteins in a sample.