Dr. Tae Hyung Kim1,2, Dr. Magdalena Swierczewska3, Dr. Yumin Oh1, Dr. AeRyon Kim6, Prof. Dr. Dong Gyu Jo2, Prof. Dr. Jae Hyung Park4, Prof. Dr. Youngro Byun5, Prof. Dr. Scheherazade Sadegh-Nasseri6, Prof. Dr. Martin G. Pomper3, Prof. Dr. Kang Choon Lee2,*, Prof. Dr. Seulki Lee1,*
1 Russell H. Morgan Department of Radiology and Radiological Science, Center for Cancer Nanotechnology Excellence, Center for Nanomedicine at the Wilmer Eye Institute, Johns Hopkins University, 400 North Broadway, Baltimore, MD 21231 (USA)
2 College of Pharmacy, Sungkyunkwan University, 300 Chonchon-dong, Jangan-gu, Suwon 440-746 (Korea)
3 Institute for NanoBioTechnology, Russell H. Morgan Department of Radiology and Radiological Science, Center for Cancer Nanotechnology Excellence, Johns Hopkins University (USA)
4 Department of Polymer Science and Engineering, Sungkyunkwan University, Suwon (Korea)
5 College of Pharmacy, Seoul National University, Seoul (Korea)
6 Department of Pathology, Johns Hopkins University (USA)
* Corresponding authors
This work was supported by the National Institute of Biomedical Imaging and Bioengineering (R00EB013450), the National Cancer Institute (U54CA151838 and T32EB013450), and the National Institute of Allergy and Infectious Diseases (2R01AI063764-06) from the National Institutes of Health and the Converging Research Center Program from the National Research Foundation in Korea (2011K000796).
Happy TRAILs to you: PEGylation of proteins through complementary interactions between a His-tag and a Ni2+ complex of nitrilotriacetic acid (NTA, see picture), a well-established practice in protein research, was used to improve the half-life of therapeutic proteins in the blood following systemic administration in vivo. Animal models show that this site-specific modification improves the efficacy of modified TRAIL proteins.
Keywords: drug screening; histidine tags; PEGylation; protein design; protein modifications