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Pegylation of recombinant mutein streptokinase from overproduction in escherchia coli BL21 and study on the fibrinolityc activity in vitro
Rachmawati H.a, Damanhuri F.a, Darfiansyah I.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]Introduction: Streptokinase is a therapeutic protein with potent thrombolytic activity. However, its use as a therapy is limited in particular by short biological half-life due to plasmin degradation in vivo. Approaches that had been developed to overcome this problem were through structural modification both chemically and genetically (mutation). Chemical modification via PEGylation process has shown better stability as indicated by longer half life and better trombolitic activity. The aim of present study is to pegylate recombinant mutein streptokinase. Methods: The recombinant mutein streptokinase was overproduced in E. coli BL21. PEGylation of protein consisted of two steps: activation of PEG with 1,1 ‘carbonyl diimidazol and conjugation of activated PEG to protein. Various factors influenced pegylation process were including incubation time and molar ratio of protein:activated PEG. Fibrinolytic activity of pegylated mutein streptokinase (PEG-streptokinase) was studied in vitro for blood clot lysis. Result: Optimum condition for PEGylation process is incubation for 48 hours with molar ratio streptokinase:activated PEG 1:400. Study on the fibrinolytic activity in vitro showed that PEG-streptokinase has better fibrinolytic activity than non-pegylated form. Conclusion: It can be concluded that recombinant mutein streptokinase was successfully pegylated with preserved and even prolonged in vitro fibrinolytic activity as compared to non-pegylated form.[/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]Clot lysis assay,Fibrinolytic,Mutan K59Q-K386Q streptokinase,PEGylation,Streptokinase[/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]