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The influence of polyethylene glycol structure on the conjugation of recombinant human interferon α2b overproduced using synthetic gene in E.coli
Rachmawati H.a, Febrina P.L.a, Ningrum R.A.a, Retnoningrum D.S.a
a Research Group of Pharmaceutics, School of Pharmacy, Bandung Institute of Technology, Indonesia
[vc_row][vc_column][vc_row_inner][vc_column_inner][vc_separator css=”.vc_custom_1624529070653{padding-top: 30px !important;padding-bottom: 30px !important;}”][/vc_column_inner][/vc_row_inner][vc_row_inner layout=”boxed”][vc_column_inner width=”3/4″ css=”.vc_custom_1624695412187{border-right-width: 1px !important;border-right-color: #dddddd !important;border-right-style: solid !important;border-radius: 1px !important;}”][vc_empty_space][megatron_heading title=”Abstract” size=”size-sm” text_align=”text-left”][vc_column_text]Interferon α2b (IFNα2b) is a cytokine which has antiviral, antiproliveration and immunomudulator activities. IFN a2b has been used as a drug for treatment of hepatitis B and C infections. However, the use of this protein is limited, as rapidly cleared by the kidney. Approaches have been made to prevent this fast renal clearance such as increasing the molecular weight of protein using inert compounds like polyethylene glycol (PEG). The aim of this research was to study the influence of PEG structure on the interferon alpha 2b pegylation. rhIFNα2b was obtained from Eschericia coli BL21 containing synthetic gene for rhIFNα2b. rhlFNa2b was pegylated with two different form of PEGs, i.e linear PEG-carbonyldiimidazole (PEG-Cl) and branched, trimethyl succinimidyl polyethylene glycol (TMS(PEG) 12). PEG-Cl was activated and characterized with Dragendorf reagent and infra red spectrophotometry. rhIFNα2b was pegylated using molar ratio 1:100 and 1:300 (protein:PEG). Characterization was performed on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). PEG 2000 was successfully activated with CDI. rhIFNα2b was only successfully conjugated with TMS(PEG) 12 resulting in polyform of pegylated proteins with 1, 3, and 5 molecules PEG attached. The structure of PEG molecule influenced the pegylation of interferon. Linear PEG activated with carbonyldiimidazole showed less reactive to interferon than branced PEG. ©JK Welfare & Pharmascope Foundation.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Author keywords” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Indexed keywords” size=”size-sm” text_align=”text-left”][vc_column_text]PEG-carbonylimidazole,Pegylation,Recombinant human IFNα2b,Trimethyl succinimidyl PEG[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Funding details” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”DOI” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][/vc_column_inner][vc_column_inner width=”1/4″][vc_column_text]Widget Plumx[/vc_column_text][/vc_column_inner][/vc_row_inner][/vc_column][/vc_row][vc_row][vc_column][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][/vc_column][/vc_row]