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All Journal HAYATI Journal of Biosciences ANNALES BOGORIENSES Narra J Makara Journal of Science Annales Bogorienses
Andri Wardiana, Andri
Research Center for Biotechnology, Indonesian Institute of Sciences Jl. Raya Bogor KM 46, Cibinong, Bogor, 16911, Indonesia
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Earth & Planetary Sciences Health Professions Immunology & microbiology Medicine & Pharmacology Public Health

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Roferon-A: A Biologic Product of Human Interferon Alpha 2a Wardiana, Andri; Ningrum, Ratih Asmana
Annales Bogorienses Vol. 19 No. 2 (2015): Annales Bogorienses
Publisher : BRIN

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Abstract

Human interferon alpha 2a (hIFNα2a) is a cytokine regulating immune system that has been used in hepatitis and cancer treatments. It has wide biological potency covering antiviral, antiproliferative and immunomodulative activities. This mini review discusses Roferon-A as a prominent commercial product of recombinant hIFNα2a which is produced in bacterial system, Escherichia coli, as therapeutic protein for several diseases, such as chronic viral Hepatitis B, Hepatitis C, melanoma, hairy cell leukemia and renal cell carcinoma. The discussion focuses on the development process with regard to its manufacturing, preclinical and clinical studies, as well as therapeutic efficacy. In addition, we also discuss biosimilar development of hIFNα2a and its potential future developments in the context of enhancing pharmacokinetic profiles.
Expression of No Affinity Tagged Recombinant Human Interferon Alpha-2a in Methylotrophic Yeast Pichia pastoris Herawati, Neng; Wardiana, Andri; Ningrum, Ratih Asmana
Annales Bogorienses Vol. 19 No. 2 (2015): Annales Bogorienses
Publisher : BRIN

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Abstract

Recombinant human interferon alpha-2a (rhIFN-2a) has been widely used for clinical therapy as antiviral, anticancer as well as immunomodulator. In this study, the open reading frame (ORF) encoding synthetic hIFN-2a was constructed to be in framed with N-terminal alpha factor secretion system in methylotrophic yeast Pichia pastoris. This research aimed to construct, express and analyse the non-affinity tagged recombinant human interferon alpha-2a in the methylotrophic yeast P. pastoris. We used pPICZB plasmid for cloning and expression vector. The confirmed recombinant plasmid containing the correct DNA sequence of hIFN-2a was linearized by SacI restriction enzyme, then transformed into P. pastoris genome using electroporation. We screened two multi-copy recombinants in YPDS plates containing Zeocin™. Buffered complex medium containing 0.5 % methanol (BMMY) was used for protein expression for 48 hours in the culture condition. The recombinant protein was purified by blue sepharose affinity chromatography. Analyses of hIFN-2a protein by SDS-PAGE and Western blot confirmed that protein band in which was observed around 19.2 kDa, was recombinant hIFN-2a. The quantification of purified rhIFN-2a using colorimetric binichoninic assay (BCA) informed that the yield was 44 mg/L culture (OD600= 2-3). 
Mini Review: GLP-1 Modification, Development, and Improvement Damai, Fedric Intan; Purwanto, Gracia Christine Lembong; Wardiana, Andri; Wisnuwardhani, Popi Hadi; Agustiyanti, Dian Fitria; Fathurahman, Alfi Taufiq; Ningrum, Ratih Asmana
Annales Bogorienses Vol. 26 No. 1 (2022): Annales Bogorienses
Publisher : BRIN

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.14203/ann.bogor.2022.v26.n1.1-12

Abstract

Diabetes Mellitus Type 2 (DM-2) is the condition where the body comes to be insensitive or even resistant towards insulin, thus resulting in deficient insulin secretion from beta cells in the pancreas. Compared with the available treatments, Glucagon-like peptide 1 (GLP-1) is considered a natural treatment to cure DM-2 due to its characteristic as an incretin hormone, where one of its functions is to improve insulin secretion and enhance beta-cell glucose sensitivity. However, GLP-1 has a limitation, which is a rapid half-life due to active degradation activities in the body. Therefore, many studies have been conducted to develop and improve the pharmacological activity of GLP-1 through structural modification and yield improvement, which are thoroughly reviewed in this paper. Structural modification of GLP-1 covers amino acid substitutions by referring to the GLP-1 analog, Exendin4, to prevent the dipeptidyl peptidase-4 (DPP-4) degradation activity and protein fusion with an additional chain to extend the half-life during administration. The yield improvement at the overexpression of GLP-1 tandem repeats sequences can increase the transcribed genes’ yield. The studies show that specific amino acid substitutions and IgG heavy chain constant regions or Fc-based fusion genes successfully enhance the pharmacological activities of GLP-1. At the same time, Pichia pastoris expression system managed to yield 219.2 mg/l target protein, where the purified target protein is capable of producing 10× yield of a single GLP analog. Further research could include the utilization of these findings in vitro as a GLP-1 analog-based therapeutics to treat DM-2.
Co-Authors Adi Santoso Adzdzakiy, Muhammad M. Agustiyani, Dian F. Agustiyanti, Dian Fitria Alamanda, Cut NC. Asyifa, Isnaini Z. Dadang Supriatna Damai, Fedric Intan Desriani Desriani Dharmayanthi, Anik B. Ema Rahmawati ERNAWATI ARIFIN GIRI-RACHMAN Fathurahman, Alfi Taufik Fathurahman, Alfi Taufiq Ferry Iskandar Fibriani, Azzania Hariyatun, Hariyatun Husnaa, Ulfatul Husnaa, Ulfatul Irawan, Herman Iryanto, Syam B. Kusumawati, Arizah Kusumawati, Arizah Marissa Angelina Nasrulloh, Mukh F. Neng Herawati, Neng Ningrum, Ratih A. Nugroho, Herjuno A. Permatasari, Fitri Aulia Popi Hadi Wisnuwardhani, Popi Hadi Prasetyoputri, Anggia Purwanto, Gracia Christine Lembong Rachman, Rifky W. RATIH ASMANA NINGRUM Ristandi, Ryan B. Robiani, Rini Saputra, Sugiyono Sativa, Alvira R. Sri Swasthikawati, Sri Stephanie, Rebecca Taharuddin, Audrey Angelina Putri Wijaya, Sri Kartika Wijaya, Sri Kartika Wisnuwardhani, Popi H. Wulandari, Ari S. Yamahoki, Nicholas Yana Rubiana, Yana Yana Rubiyana, Yana Yanthi, Nova D.