Glycosylation is among the most complex and diverse modification of proteins and lipids found in all forms of biological life and advanced mass spectrometry is central in the analysis of these structures.
Every living cell is composed of nucleic acids, proteins, lipids, low molecular weight metabolites and glycans. The basic exploration and our understanding of nucleic acids and proteins as well as the subsequent technical revolution in molecular biology has advanced those fields tremendously during the last decades. The study of glycans and glycoconjugates has been left behind, partly, this may be explained by the greater structural complexity and diversity of this class of molecules. Glycosylation demands a complex nomenclature and a need for multiple advanced technologies for preparation and analysis of glycoconjugates, and an in-depth knowledge of systems biology and medicine.
Analogous to proteomics, glycoproteomics is based on advanced mass spectrometry technologies that has evolved as the method of choice for global or directed analysis of glycoproteins and proteoglycans in biological tissue. The concept is to characterize the glycans as well as their exact attachment sites on specific peptides, identified by their unique amino acid sequences. To accomplish this a series of enrichment strategies, ionization techniques as well as bioinformatic tools have now become available.
Support within glycoproteomics at BioMS include:
- Global identification of glycopeptides
- Structural characterization of N- and O-linked glycopeptides
- Relative quantification of glycopeptides