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Recombination therapeutic proteins are most glycosylated and the protein glycosylation may have an effect on the structure and function of therapeutic proteins. With the highly specialized equipment and experienced expert staff, Creative Biolabs can provide a full range of custom synthesis services, including glycans synthesis, glycopeptide synthesis, and glycoprotein synthesis, with the highest quality and the most competitive price for global clients.
Protein glycosylation is a common posttranslational modification that plays a very important role in various biological processes including cell-cell recognition, immune response, and cellular signal transduction. Approximately more than 50% of proteins undergo glycosylation modification. Importantly, more than 60% of those recombinant therapeutic proteins are glycosylated and glycosylation pattern has an effect on the efﬁcacy, half-life, stability, and safety of therapeutic proteins. In order to investigate the relationship between structure and function of glycoproteins, it is required to synthesize homogeneous glycoproteins with defined oligosaccharide side chains.
Unlike nucleic acid and protein, biosynthesis of glycopeptide or glycoprotein is non-template. Hence, glycoproteins always exist as heterogeneous mixtures with different glycan structures and it is difficult to synthesize homogenous glycoproteins in vitro. Over the past years, different strategies have been developed for obtaining the homogenous glycoproteins including chemical and chemoenzymatic methods. This not only helps to investigate the structure and function of glycoproteins but also facilitates the development of therapeutic recombination glycoproteins.
Fig.1 The different types of glycans produced in different organisms.
Chemical synthesis is a common method that utilizes chemical link coupling two substances. This method has been applied for glycopeptide and glycoprotein synthesis. Currently, there have two strategies for glycopeptides/glycoproteins synthesis. The first is to form a linkage between glycan and protein early to form glycopeptide building blocks that may then be assembled. The second is the construction of the linkage at the later stages of synthesis once the protein scaffold is in place. In addition, chemical method is also used for small oligosaccharide side chains, such as those found in O-linked glycans.
It is known that enzymes exert an essential in the biosynthesis of macromolecule via promoting synthetic rate. During the process of glycosylation, many enzymes such as glycosidases and glycosyltransferases have been found in vivo to promote the production of glycopeptide and glycoproteins. Moreover, these enzymes also function in vitro glycosylation processing. Now a variety of enzymes have been available through isolation from natural sources or by heterologous overexpression in exogenous hosts. Furthermore, these enzymes have been shown to accept saccharides, glycolipids, and glycoproteins as substrates. By using an excess of enzyme, high yielding reactions are possible even if the substrates are poor.
Fig.2 Biosynthetic pathways for glycoproteins (Wang, 2014).
Creative Biolabs is an omnibearing service provider of custom synthesis. Our professional experts have extensive experience in glycoprotein synthesis. We are committed to offering the most comprehensive custom synthesis services with the highest quality and most competitive price to our worldwide clients. In order to meet every specific need of our clients’ research and project development, our scientists are pleased to tailor the best-fit approach to provide a comprehensive custom synthesis service. Our services include:
Equipped with advanced technologies and professional scientists, we are confident to provide comprehensive and high-quality custom synthesis services. We believe that our high-quality services will help you get through many thorny issues in custom synthesis. Please feel free to contact us for more details.