Glycosylation is generally known as a form of co-translational and post-translational modifications of proteins. More than 50% of proteins expressed in living cells are considered to be glycosylated. In the biopharmaceutical industry, cell culture systems derived from mammalian cells are used for the production of glycoprotein therapeutics because glycans play prominent roles in affecting therapeutic efficacy based on their stability. Although many investigations show the possible roles of glycans on glycoproteins, the detailed functions of glycans are still uncharted because of the complexity of glycan structures and the difficulty of manufacturing a homogeneous glycoform profile that can be screened for systematically.
GlyTech, Inc. has been focusing on human type asparagine linked glycans (N-glycans), and has established a large-scale manufacturing process to prepare highly purified and characterized human type N-glycan libraries in collaboration with Prof. Kajihara (Osaka University, Japan).1) Furthermore, we have developed glycosylation technologies which can be applied for producing not only natural glycoproteins, but also highly qualified and advanced glycopeptide/glycoprotein therapeutics. Attaching several glycans to peptides and proteins is an unique technology, permitting generation of homogeneous glycopeptides and glycoproteins with optimized glycan structures at desired glycosylation positions. Our technologies are applicable to novel drug discovery and can contribute to the advancement of human health.
1)Y. Kajihara, Y. Suzuki, N. Yamamoto, K. Sasaki, T. Sakakibara, R. R. Juneja; Prompt Chemoenzymatic Synthesis of Diverse Complex Type Oligosaccharides and its Application to the Solid Phase Synthesis of a Glycopeptide Having Asn-linked Sialyl-undeca and Asialo-nonasaccharides. Chem. Eur. J. (2004), 10, 971-985.