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, researchers from the laboratories of Martin Pomper (radiology oncology) and Seulki Lee (radiology, Center for Nanomedicine) at the Johns Hopkins School of Medicine and developed a simple method to validate protein drugs in animal models, said Lee. 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. “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.
Authors on this paper include Tae Hyung Kim, Magdalena Swierczewska, Yumin Oh, AeRyon Kim, Dong Gyu Jo, Jae Hyung Park, Youngro Byun, Scheherazade Sadegh-Nasseri, Martin G. Pomper, Kang Choon Lee, Seulki Lee. Author affiliations include the departments of Radiology and Pathology at the Johns Hopkins School of Medicine, the Johns Hopkins Center of Cancer Nanotechnology Excellence, the Johns Hopkins Institute for NanoBioTechnology, Center for Nanomedicine and collaborators at Sungkyunkwan University and Seoul National University, both in Korea.
Reference: Kim, T. H., Swierczewska, M., Oh, Y., Kim, A., Jo, D. G., Park, J. H., Byun, Y., Sadegh-Nasseri, S., Pomper, M. G., Lee, K. C. and Lee, S. (2013), Mix to Validate: A Facile, Reversible PEGylation for Fast Screening of Potential Therapeutic Proteins In Vivo. Angew. Chem. Int. Ed.. Vol. 52, Issue 27, pages 6880-6884, doi: 10.1002/anie.201302181