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Pegylation and Glycosylation

Pegylation is another technique that we use for the monoclonal antibody or for recombinant DNA in that regard. Pegylation refers to the covalent attachment of PEG to peptide and proteins. By doing so, it reduces the degradation by proteolytic enzymes. It reduces renal filtration by increasing the molecular size of the polypeptide. It increases water solubility making it less prone to adsorption to the container wall or syringe needle. Another technique that we use is the so-called glycosylation. It’s the covalent attachment of carbohydrate or the glycans to the protein surface. By doing so, it stabilizes the protein. It decreases the circulatory turnover and clearance rate. Again so that the antibody or the recombinant DNA gets to stay in the body for longer.
And it increases subcutaneous absorption, for example. And improve distribution. So to quickly summarize, we use chimerization to modify the structure of the monoclonal antibody. We use glycosylation or insulation to modify the structure of the recombinant DNA product or the monoclonal antibody product. And this slide summarized it. This is the pegylation. This is the source of Polyethylene glycol. This is glycosylation. And this is the glycans. So we use chimerization, pegylation, and glycosylation to modify the structure of the monoclonal antibody, or the recombined DNA to make them stay in the system longer so that they have a better chance to work their way to improve the conditions of the patient.

Pegylation and glycosylation are biochemical processes used to improve the therapeutic function of a protein. Typically, the PEG moiety or the glycosylic moiety offers advantages for increasing the protein’s solubility, stability and circulating half-life (residence time).

Two biochemical methods are commonly used to improve the in-vivo function of the therapeutic proteins. Pegylation, in which a functional group (primary amine) on a protein is reacted with a polyethyleneglycol polymer (PEG) to form a protein–PEG conjugate. Glycosylation, in which a carbohydrate (glycosyl donor) is attached to the hydroxyl (o-linked) or amino group (N-linked) of a protein.

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