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Journal of Microbiology and Biotechnology Reports

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Development of Agonists and Antagonists of Glycoproteins Using Site-Directed Mutagenesis and Gene Fusion

Author(s): Fuad Fares

One major issue regarding the clinical use of many peptides is their short half-life due to the rapid clearance from the circulation. To overcome this problem previous studies ligate the interested proteins to polyethylene glycol or to IgG-FC fragment. Here we used other strategy, of ligation the signal sequence of O-linked oligosaccharides to the coding sequence of the interested protein. The cassette gene that has been used contains the sequence of the carboxyl-terminal peptide (CTP) of human chorionic gonadotropin  subunit (hCG). The CTP contains 28 amino acids with four O-linked oligosaccharide recognition sites.Using this strategy, the CTP sequence was ligated to the coding sequence of follitropin (FSH), thyrotropin (TSH), erythropoietin (EPO), growth hormone (GH) and thus to increase the longevity and bioactivity of these proteins in-vivo. Interestingly, the new analogs of FSH and GH found to be not immunogenic in human and it is already passed successfully clinical trials phase III. Moreover, the European Commission (EC) for treatment of fertility approved FSH long-acting (ELONVA) and it is already used in many countries
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