Thursday, September 18, 2014

Site-Specific Characterization of Glycosylation on Protein Drugs

Today, we feature an article from our partners at BioProcess International Magazine. This is an excerpt from the article Site-Specific Characterization of Glycosylation on Protein Drugs.

BPI_A_141206AR05_O_F0001gA large proportion of biotherapeutic products are glycoproteins. These include erythropoietin and other cytokines, antibodies, glycosyltransferases, and glycosidases, which together generate billions of dollars in sales worldwide. Such drugs are inherently complex. As new treatments emerge and biosimilars are evaluated, the need to better understand their molecular structures is more acute than ever.

Therapeutic glycoproteins are typically produced as recombinant products in cell culture systems. Glycosylation is of major importance during development of these drugs because their glycan chains markedly affect product stability, activity, antigenicity, and pharmacodynamics. A detailed description of the structural features for such carbohydrate-containing molecules is increasingly expected as part of their new drug applications (NDAs) or comparability protocols.

Read the full article here.

You can find out more about topics like this and meet and network with other professionals in the bioprocessing field at this year's BioProcess International Conference and Exhibition.  As a reader of this blog, when you register to join us October 20-23 in Boston, you are eligible to receive 20% off the standard rate when you mention code BPI14BLOG.

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