Site-Selective Glycosylation
Site-selective glycosylation is considered as an effective method that was widely used in glycoproteins. As an expert in the field of glycoprotein research, Creative Biolabs has mastered a variety of site-selective glycosylation technologies. We can provide efficient site-selective glycosylation services for customers all over the world and our professional scientists can help you solve various challenges in the project to speed up your project.
Background of Site-Selective Glycosylation
Surface glycoproteins are closely related to microbial virulence, inflammation, and immune response. In addition, the correct glycosylation of the protein is important for its expression and stability. Moreover, glycoproteins occur naturally in many forms, they have the same peptide backbone, but the properties and sites of glycosylation are different. In order to explore these key characteristics, a large number of methods have been used to prepare pure glycosylated proteins as well as non-natural variants of glycoproteins.
Introduction of Site-Selective Glycosylation
In general, the protein backbones of protein isoforms are the same, but the properties of glycosylation sites are quite different. To better understand the relationship of structure and function in glycoproteins, complete control of glycans and glycosylation sites is required. This problem can be solved by a combination of site-directed mutagenesis and chemical modification. The procedure involves introducing certain amino acids as tags into preselected positions within a given protein by site-directed mutagenesis followed by modified with specific compound reagents.
Applications
After years of development, the site-selective method has been widely used in basic research and biomedical applications. PEGylation is a common strategy to extend the half-life of therapeutic proteins. To develop effective alternatives, site-based glycosylation is proposed. This method mainly relies on carbohydrates of different sizes for rapid site-selective glycosylation of proteins. In addition, this strategy allows easy site-selective glycosylation of the desired protein using glycans of different sizes and is not limited by the size of oligosaccharides. What's more, in some studies, certain glycoproteins without natural cysteine can be modified by site-directed mutagenesis at a predetermined position in their sequence, which can be modified by glycosylation. It is worth noting that a simple cysteine-directed glycosylation strategy has been successfully developed, which will accelerate the study of the effect of glycosylation on protein translation modification. In addition to the above examples, there are many application examples of this strategy in medical research.
Understanding the selectivity and predictability of protein glycosylation is an important trend. Creative Biolabs has applied a variety of new methods based on enzymatic synthesis to glycoprotein synthesis. Based on our rich experience and advanced platform, we can provide customers with a variety of glycoprotein synthesis and testing services. If you have questions about site-selective glycosylation or custom glycoprotein synthesis, please contact us in time.
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