Improvement of in vitro stability and pharmacokinetics of hIFN-α by fusing the carboxyl-terminal peptide of hCG β-subunit
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- 作者：Natalia Ceaglioa ; nceaglio@fbcb.unl.edu.ar" class="auth_mail" title="E-mail the corresponding author ; Agustina Gugliottaa ; Marí ; a Belé ; n Tardivob ; Dianela Craveroa ; Marina Etcheverrigaraya ; Ricardo Kratjea ; Marcos Oggeroa
- 关键词：hIFN-α ; human interferon alpha ; hCG ; human chorionic gonadotropin ; CTP ; carboxyl-terminal peptide ; LH ; luteinizing hormone ; FSH ; follicle-stimulating hormone ; TSH ; thyrotropin ; EPO ; erythropoietin ; LV ; lentiviral ; LVP ; lentiviral particle ; Cmax ; maximum plasma concentration ; Tmax ; time to reach Cmax ; t1/2 ; terminal half-life ; AUC ; area under curve ; CLapp ; apparent clearance ; 2-AB ; 2-aminobenzamide
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：10 March 2016
- 年：2016
- 卷：221
- 期：Complete
- 页码：13-24
- 全文大小：1235 K
文摘
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A strategy based on the fusion of carboxyl-terminal peptide (CTP) of hCG was applied to hIFN-α2b.
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CTP remarkably improved the rhIFN-α2b stability after thermal and plasma protease treatment.
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CTP fusion significantly enhanced the pharmacokinetic properties of rhIFN-α2b.
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CHO-derived O-glycans of CTP resemble hCG glycans found in human normal cells.