Improvement of in vitro stability and pharmacokinetics of hIFN-α by fusing the carboxyl-terminal peptide of hCG β-subunit

•A strategy based on the fusion of carboxyl-terminal peptide (CTP) of hCG was applied to hIFN-α2b.•CTP remarkably improved the rhIFN-α2b stability after thermal and plasma protease treatment.•CTP fusion significantly enhanced the pharmacokinetic properties of rhIFN-α2b.•CHO-derived O-glycans of CTP...

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Veröffentlicht in:	Journal of biotechnology 2016-03, Vol.221, p.13-24
Hauptverfasser:	Ceaglio, Natalia, Gugliotta, Agustina, Tardivo, María Belén, Cravero, Dianela, Etcheverrigaray, Marina, Kratje, Ricardo, Oggero, Marcos
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antiviral Agents - metabolism Antiviral Agents - pharmacokinetics Biomedical materials Carboxyl-terminal peptide Cattle Cell Line CHO Cells Chorionic Gonadotropin, beta Subunit, Human - chemistry Chorionic Gonadotropin, beta Subunit, Human - genetics Cricetulus Cytokines Cytostatic Agents - metabolism Cytostatic Agents - pharmacokinetics Drug Stability Half life hCG β-subunit HEK293 Cells Human Humans in vitro protein stability In vitro testing Interferon-alpha - genetics Interferon-alpha - metabolism O-Glycosylation Peptide Fragments - genetics Peptide Fragments - metabolism Peptides Pharmacokinetics Rats Recombinant human interferon alpha Recombinant Proteins - metabolism Recombinant Proteins - pharmacokinetics Recombinant Proteins - secretion Stability Surgical implants
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