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Protein Characterization Glycosylation

Glycosylation

 

IMG_4714Let us simplify the complexity

Do you need to investigate glycosylation to ensure protein structural integrity during drug development? Would you like to see if any molecular alterations have taken place during fermentation, purification or storage?

Proteins that have undergone glycosylation are incredibly complex. Several glycans may be attached to numerous amino acids, and each glycan will show unique and sometimes unexpected branching.

You’ll want only the most experienced researchers looking at this in your proteins because of the intricacy involved. This is where our long history in specialised biopharmaceutical protein analysis is of benefit to you.

Although glycosylation analysis is a fairly new field of research, we have such an in-depth understanding of protein structure that we’re already unparalleled in terms of the level of detail, such as rigorous structural information, we can provide.

We apply a selection of techniques, depending on your circumstances, in order to obtain a complete overview of the glycans in your proteins. They include high resolution mass spectrometry, HPLC and electrophoretic methods.

Mass spectrometry is an important technique because of its high selectivity and sensitivity. It also provides information quickly. The mass spectrometry strategy we’ll employ will depend on the level of structural information you require. A typical strategy is shown below.

 

Once the analyses are complete, we package the results to tell you exact glycosylation sites and how the glycans are or are not contributing to the product you’re developing.

And we do all this at cost-effective prices.

You can choose from the following types of analysis:

  • N-linked glycosylation, to explore the attachment of N-linked glycans at the end of enzymes.
  • O-linked glycosylation, to investigate the more complex addition of O-linked glycans, which occurs later in protein processing.
  • Sialic acid content, to determine the type and quantity of sialic acid present at any stage of drug development, information which is helpful in further glycosylation analysis.
  • Monosaccharide content, to determine the composition and quantity of N- and O-linked glycosylation.
  • Glycosylation site, to work out exactly where glycans are attached to your proteins, because normally not all available sites will be occupied.

Characterizing glycosylation is a key requirement of ICH Q6B.

 

Technical information

Protein glycosylation is a post-translational modification that alters a protein’s structure or function. It is a very common and biologically relevant modification that may be directly involved in the formation of diseases. It also plays an important role in altering the pharmacokinetics by stabilizing the protein conformation, improving solubility or protecting from proteases.

The main challenge in the analysis of protein glycosylation is its structural complexity, which arises from a combination of factors such as:

  • Multiple glycosylation sites per protein
  • Multiple glycan structures attached to each site
  • The complex, branched structure of glycans

 

Your contact for Glycosylation at Protagen Protein Services GmbH

Marcus-Mreyen

Marcus Mreyen

Director Business Development
Our business development team will be happy to assist you with your project.

Phone: +49 (0) 231 9742-6100
Email: salesproteinservices@ProtagenProteinServices.com