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Posted: Jan 24, 2014

Making therapeutic proteins last longer

(Nanowerk News) Proteins are responsible for pretty much everything in the human body. When there is a problem with the proteins, it usually leads to disease. Protein therapy shows enormous potential for treating disease. But sometimes the proteins in a therapeutic treatment break down or are metabolized before they ever reach their target destination.
In a recent paper published in Angewandte Chemie ("Mix to Validate: A Facile, Reversible PEGylation for Fast Screening of Potential Therapeutic Proteins In Vivo"), researchers from the laboratories of Martin Pomper, professor of radiology oncology and CCNE co-director, and Seulki Lee, assistant professor of radiology at the Johns Hopkins School of Medicine, developed a simple method to validate protein drugs in animal models. An illustration related to the paper appeared on the cover of the journal.
"We show that we can extend the half-life, that is, the amount of time the drug stays in the blood, while maintaining the activity of the model protein drug, TRAIL," said one of the lead authors Maggie Swierczewska, a post doctoral fellow in the Pomper lab. "This has great implications for drug screening and validation methods, especially for the growing protein drug market."
According to the paper, by attaching a molecule of polyethylene glycol (PEG) to certain sites on the TRAIL protein drugs through an already well known method, the half-life of the drug could be extended without affecting its beneficial activity.
Source: National Cancer Institute
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