Protein Glycoengineering

In the field of Glycoengineering, CD BioGlyco has accumulated rich experience. We have successfully developed a variety of first-class protein glycoengineering strategies to meet our client's research needs.

Properties of Protein

Recombinant proteins are an important class of biological macromolecules. In the field of medicine, recombinant proteins have been developed for the treatment of cancer, autoimmune diseases, contagious diseases, genetic diseases, etc. Glycosylation is the process of binding carbohydrates to proteins or lipids under the control of enzymes. It is generally divided into two main types: 1) N-glycosylation (attached to the nitrogen of the asparagine or arginine side chain); 2) O-glycosylation (attached to the hydroxyl oxygen of the side chain of serine, threonine, tyrosine, hydroxylysine, or hydroxyproline). Glycosylation plays an important role in regulating protein properties. The size, mass, stability, solubility, intracellular transport, and immunogenicity of protein are all closely related to the quantity and structure of glycans during glycosylation. In addition, glycosylation is also related to the biological activity and clearance rate of therapeutic proteins, which in turn affects the efficacy of therapeutic proteins. Therefore, the glycosylation process should be carefully controlled during the production of therapeutic proteins to achieve the best therapeutic effect.

Fig.1 Glycoengineering strategies to install chemical handle into the N-glycans of therapeutic proteins.Fig.1 Glycoengineering strategies to install "chemical handle" into the N-glycans of therapeutic proteins. (Dammen-Brower, et al., 2022)

In recent years, scientists have developed a glycoengineering approach to modify glycans involved in protein glycosylation to enhance therapeutic effects. There are generally two strategies for protein glycoengineering: 1) Changing the number and location of glycosylation sites; 2) Changing the glycan structure (including linkage type, chain length, and composition) of individual glycosylation sites. When appropriate glycosylation sites and glycan structures are selected, protein glycoengineering strategies simultaneously improve many different properties of proteins. Thus, this method is being explored by more and more scientists.

Protein Glycoengineering at CD BioGlyco

Glycoengineering has attracted considerable attention from scientists over the past few decades as an important approach to improving the efficacy of therapeutic proteins. At CD BioGlyco, we have established a professional In Vitro Glycoengineering platform to provide first-class and high-quality protein glycoengineering services for global clients. Our glycoengineering strategies include but are not limited to:

1) Incorporate additional glycosylation sites into the protein backbone by site-directed mutagenesis, thereby improving the activity and half-life of therapeutic glycoproteins.

2) The target glycans are introduced into specific glycosylation sites by site-directed mutagenesis. These glycans are then reacted with modified glycans containing appropriate functional groups through orthogonal chemoselective linkages, thereby enhancing the biological activity of therapeutic glycoproteins.

3) Deglycosylation of glycoproteins produced in host cells to produce homogeneous N-acetylglucosamine (GlcNAc)-containing proteins. Homologous glycans are then extended to obtain glycan-defined glycoproteins.

Advantages of Us

  • Modification strategies to introduce additional glycosylation sites
  • Changing the glycan structure of individual glycosylation site
  • Chemoenzymatic glycosylation remodeling
  • Professional in vitro glycoengineering platform

CD BioGlyco is a leading service provider specializing in glycoengineering services. We have established a professional in vitro glycoengineering platform for protein glycoengineering. If you are interested in our protein glycoengineering, please contact us for more details without any hesitation.

References:

  1. Dammen-Brower, K.; et al. Strategies for glycoengineering therapeutic proteins. Frontiers in Chemistry. 2022, 10.
  2. Costa, A.R.; et al. Glycosylation: impact, control and improvement during therapeutic protein production. Critical reviews in biotechnology. 2014, 34(4): 281-299.
This service is for Research Use Only, not intended for any clinical use.

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