TY - GEN
T1 - Apoptin gene optimization in Escherichia coli
AU - Sahlan, Muhamad
AU - Wiratama, Ihsan
AU - Hermansyah, Heri
AU - Wijarnako, Anondho
AU - Gumelar, Mohamad Teguh
AU - Yohda, Masafumi
N1 - Funding Information:
This article’s publication is partially supported by the United States Agency for International Development (USAID) through the Sustainable Higher Education Research Alliance (SHERA) Program for Universitas Indonesia’s Scientific Modeling, Application, Research, and Training for City-centered Innovation and Technology (SMART CITY) Project, Grant #AID-497-A-1600004, Sub Grant #IIE-00000078-UI-1.
Publisher Copyright:
© 2019 Author(s).
PY - 2019/4/9
Y1 - 2019/4/9
N2 - Apoptin is intensively studied for its potential as a therapeutic protein for cancer treatment since it is capable of inducing apoptosis specifically in cancer cells. Production of apoptin gene on a larger scale is important for the further application, and currently being studied by researchers around the world. In this research, chicken anemia virus apoptin optimized genetically for expression in Escherichia coli and modified using (His)6 tag, (Arg)8 tag, and HlyA tag intended for purification needs, penetration enhancement, and secretion from bacterial host to the growth media. Removal of (His)6 tag and HlyA tag were designed using a specific thrombin proteolytic site, while (Arg)8 tag was preserved. The gene designed, optimized and constructed in vector pET9a, then analyzed using Agarose Electrophoresis and Sequencing. The DNA sequencing result shows that the designed gene has successfully constructed.
AB - Apoptin is intensively studied for its potential as a therapeutic protein for cancer treatment since it is capable of inducing apoptosis specifically in cancer cells. Production of apoptin gene on a larger scale is important for the further application, and currently being studied by researchers around the world. In this research, chicken anemia virus apoptin optimized genetically for expression in Escherichia coli and modified using (His)6 tag, (Arg)8 tag, and HlyA tag intended for purification needs, penetration enhancement, and secretion from bacterial host to the growth media. Removal of (His)6 tag and HlyA tag were designed using a specific thrombin proteolytic site, while (Arg)8 tag was preserved. The gene designed, optimized and constructed in vector pET9a, then analyzed using Agarose Electrophoresis and Sequencing. The DNA sequencing result shows that the designed gene has successfully constructed.
KW - apoptin
KW - codon optimization
UR - http://www.scopus.com/inward/record.url?scp=85064820028&partnerID=8YFLogxK
U2 - 10.1063/1.5096733
DO - 10.1063/1.5096733
M3 - Conference contribution
AN - SCOPUS:85064820028
T3 - AIP Conference Proceedings
BT - 3rd Biomedical Engineering''s Recent Progress in Biomaterials, Drugs Development, and Medical Devices
A2 - Wulan, Praswasti P.D.K.
A2 - Gozan, Misri
A2 - Astutiningsih, Sotya
A2 - Ramahdita, Ghiska
A2 - Dhelika, Radon
A2 - Kreshanti, Prasetyanugraheni
PB - American Institute of Physics Inc.
T2 - 3rd International Symposium of Biomedical Engineering''s Recent Progress in Biomaterials, Drugs Development, and Medical Devices, ISBE 2018
Y2 - 6 August 2018 through 8 August 2018
ER -
