Chemical Synthesis of Glycoproteins

Chemical Synthesis of Glycoproteins

CD BioGlyco has a variety of advanced technology platforms and customized glycoprotein synthesis services. The high-quality samples we provide can perform well in customers' research. We have confidence to be your essential research assistant in the field of glycobiology.


As one of the most common post-translational modifications, glycosylation can profoundly affect the folding, stability, and intracellular transportation of proteins. Moreover, linked glycans can directly participate in numerous biological recognition processes: cell adhesion, signal transduction, development, host-pathogen interaction and immune response.

The structural diversity of glycoproteins lays the molecular foundation for a variety of biological functions. However, the structural heterogeneity also brings great challenges to elucidate the biological functions of glycoproteins. Unfortunately, it is still difficult to control glycosylation to a well-defined glycoform during protein expression, and current chromatographic techniques cannot separate different glycoprotein glycoforms on a practical scale. The urgent need for well-defined homogeneous glycoproteins for functional research and biomedical applications has stimulated considerable interest in developing methods for the preparation of homogeneous glycoproteins.

The conventional solid-phase peptide synthesis (SPPS) protocols have been used to prepare small to middle-sized N- and O-glycopeptides. Due to the low coupling efficiency, the poor solubility of the protected peptides, and the sensitivity of the O-glycosidic bond to acid hydrolysis under strong acidic conditions required for the final global peptide de-protections, this method is problematic in extending glycopeptides.

Fig 1. Chemical synthesis of homogeneous glycoproteinsFig 1. Chemical synthesis of homogeneous glycoproteins (Li, C.; Wang, L.X. 2018)


The invention of natural chemical linkage (NCL) for total chemical synthesis of proteins revolutionized protein chemistry. The application of NCL and its modified versions for the linkage of peptide and glycopeptide allows us to synthesize large homogenous glycoproteins.

In addition, expressed protein ligation (EPL) has been successfully used in glycoprotein synthesis, in which a intact protein thioester or a protein domain containing N-terminal Cys is recombinantly expressed and used as a ligation partner. CD BioGlyco combines EPL and NCL to further overcome the size limitation of traditional NCL. It combines the advantages of molecular engineering and chemical peptide synthesis, and non-natural amino acids and chemical tags can be introduced into proteins at designated locations.


  • Glycoproteins structure & function research
  • Development of therapeutic glycoproteins
  • Research on glycoprotein-related cellular activities

Advantages of Us

  • Multiple advanced chemical synthesis technology platforms
  • Customizable modifications
  • Able to synthesize complex glycoproteins
  • 24 hours after-sales service

CD BioGlyco has many years of successful experience in glycoproteins synthesis. Our professional and rigorous synthetic chemists can provide customers with high-quality and homogeneous glycoforms glycoproteins.

Customers can contact our employees directly and we will respond promptly. If you are interested in our services, please contact us for more detailed information.


  1. Li, C.; Wang, L.X. Chemoenzymatic methods for the synthesis of glycoproteins. Chem Rev. 2018, 118(17): 8359-8413.
This service is for Research Use Only, not intended for any clinical use.

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