Post-translational modification is a group modification that occurs in the side chain or certain sites of protein due to covalent bonding or the catalysis of certain enzymes. Post-translational modifications of proteins mainly include glycosylation, phosphorylation, acetylation, and ubiquitination. CD BioGlyco provides custom glycosylation services of proteins for our global customers based on biochemistry and organic chemistry.
Glycosylation, the enzymatic process of attaching glycans to proteins or other organic molecules, occurs at sites such as the endoplasmic reticulum (ER) and the Golgi apparatus. Protein glycosylation is one of the most important post-translational modifications of proteins, and the realization of protein functions is closely related to glycosylation. Glycosylation modification plays an important role in the spatial conformation, biological activity, transport, and localization of proteins, and participates in specific biological processes such as receptor activation, cellular communication, and signal transduction. Currently, many clinical biomarkers and therapeutic targets are glycoproteins. Therefore, the field of glycobiology has become one of the most promising research fields in life sciences.
Fig.1 An overview of the process of N-glycosylation. (Ho, 2016)
Glycosylation is divided into N-glycosylation, O-glycosylation, C-glycosylation, glycation, and phosphoglycosylation. N-glycosylation is the most common type of glycosylation, and glycans are linked to the NH2 of asparagine residues in the ER. O-glycosylation occurs on threonine (Thr) and serine (Ser) side chains in the Golgi apparatus and plays an important role in cell biology. C-mannosylation is a distinct method of glycosylation whose biological function is unclear. To date, C-mannosylation has been detected in rat liver microsomes and various cell lines. Glycation, the attachment of proteins and phospholipids to the glycan core, is widely detected on surface glycoproteins in archaea and eukaryotes. The glycosylation of glycans linked to Thr or Ser via phosphodiester bonds is called phosphoglycosylation, and this glycosylation is restricted to slime molds and parasites.
We can achieve protein glycosylation through biochemical reactions catalyzed by various glycosidases and glycosyltransferases. For example, bovine ribonuclease B glycoproteins (RNase B) modified with high-mannose or complex N-glycan is synthesized by glycan remodeling.
We can achieve O-linked protein glycosylation by organic chemistry. Due to the precision and flexibility of organic chemistry, this method can be used not only to modify the structure of glycoproteins at the atomic level but also to prepare glycosylated proteins containing any glycosylation site and any glycan.
CD BioGlyco is a leader in the field of glycan remodeling, providing our customers with high-quality, cost-effective, and hassle-free custom glycosylation of proteins. If you are interested in our services, please feel free to contact us, we are looking forward to being your indispensable assistant in this field.