Protein Glycosylation
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Protein Glycosylation

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As a leading supplier of bioactive peptides, we provide comprehensive services for glycosylated peptide development and production from mg to kg quantities to meet your project needs.

What is glycosylation?

Glycosylation is the most common post-translational modification of proteins in eukaryotic cells. As one of the most important recognition signals, glycosylated proteins and peptides are involved in much intracellular communication, such as apoptosis, cell growth regulation, infection process, and immunological differentiation.

Advantages of glycosylated peptides

  1. Increased bioavailability.
  2. Increased metabolic stability.
  3. Targeting specific tissues and organs.
  4. Reduced clearance.
  5. Enhanced receptor binding.
  6. Promote activity.
  7. Maintain the overall physical properties of the peptide (precipitation, aggregation, thermal and kinetic denaturation).

Classification of glycosylation

Protein glycosylation can be categorized into four main categories mainly according to various glycosidic linkages between the amino acid and the sugar, including

  1. N-linked glycosylation.
  2. O-linked glycosylation.
  3. C-Mannosylation.
  4. Glycophosphatidlyinositol (GPI) anchor attachments.

Structures of N-glycans and O-glycans
Figure 1: Structures of N-glycans and O-glycans.

Common services of monosaccharide, disaccharide, polysaccharide

Creative peptides recognizes that all our clients have specific and unique requirements. We provide common monosaccharide, disaccharide and polysaccharide services. Other glycosylation modifications (sialic acid, fucose, etc.) can also be performed on the main chain and side chain of the polypeptide.

  1. Related Carbohydrates


NameCASFormulaAcetate Groups Removed
beta-D-Glucose pentaacetate604-69-3C16H22O11Yes&No
Gluconic acid526-95-4C6H12O7NO
6-phosphogluconic acid921-62-0C6H13O10PNO


NameCASFormulaAcetate Groups Removed
beta-D-Galactose pentaacetate4163-60-4C16H22O11Yes&No


NameCASFormulaAcetate Groups Removed
Fmoc-L-Ser(ManNAc)-OH  Yes&No
Fmoc-Thr(ManNAc)-OH  Yes&No
D-Mannopyranose tetraacetate140147-37-1C14H20O10Yes&No

1. Spiro, R. G. (2002). Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology, 12(4), 43R.
2. Chen, S. A., Lee, T. Y., & Ou, Y. Y. (2010). Incorporating significant amino acid pairs to identify o-linked glycosylation sites on transmembrane proteins and non-transmembrane proteins. BMC Bioinformatics, 11(1), 536-0.
3. Costa, A. R., Rodrigues, M. E., Henriques, M., Oliveira, Rosário, & Azeredo, J. (2014). Glycosylation: impact, control and improvement during therapeutic protein production. Critical Reviews in Biotechnology, 34(4), 281-299.
4. Ricardo J. Solá, & Griebenow, K. (2009). Effects of glycosylation on the stability of protein pharmaceuticals. Journal of Pharmaceutical Sciences, 98(4), 1223-1245.
5. Wolfert, M. A. & Boons, G. J. (2013). Adaptive immune activation: glycosylation does matter. Nature Chemical Biology, 9(12), 776-784.

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