cover
Article Per Year (5 Year)
All
Home Page
OAI Link
Editorial Team
Contact
Reviewer
Google Scholar
Contact Name
Dr. Nuri Nurlaila Setiawan
Contact Email
editor3bio@sith.itb.ac.id
Phone
+62222511575
Journal Mail Official
support3bio@sith.itb.ac.id
Editorial Address
Sekolah Ilmu dan Teknologi Hayati, Institut Teknologi Bandung Labtek XI, Jl. Ganesha 10 Bandung 40132 West Java - Indonesia
Location
Kota bandung,
Jawa barat
INDONESIA
3BIO: Journal of Biological Science, Technology and Management
Published by Institut Teknologi Bandung
ISSN : -     EISSN : 26558777     DOI : http://dx.doi.org/10.5614%2F3bio.2020.2.1
Core Subject : Science, Agriculture, Engineering,
Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Immunology & microbiology Neuroscience
3Bio: Journal of Biological Science, Technology and Management is an interdisciplinary peer-reviewed journal in a wide aspect related to the field of life sciences and other related fields of study. The journal aims to promote scientific discourse and disseminate research on various branches and applications of bio-science, biotechnology and bio-based management. This journal invites original empirical research, literature reviews, theoretical or methodological contributions, or short communications on, but not limited to, the following topics: - Ecology and Biosystematics - Microbiology - Genetics and Molecular Biology - Animal Development and Physiology - Plant Development and Physiology - Entomology - Biomedical science - Biochemistry - Agronomy - Forestry - Bioengineering - Bioethics - Management of Biological Resources The journal also invites contributions from other associated disciplines. This journal is an open-access journal. Readers may read, download, copy, distribute, print, search, or link to the full texts of these articles without any charge, provided that readers acknowledge the Creative Commons attached to the articles. All submitted papers are reviewed by at least two referees before being accepted for publication, following a double-blind review process. This journal is delivered in an academic English and rigorously edited to provide a quality standard of a scientific journal. This journal is managed by the School of Life Sciences and Technology, Institut Teknologi Bandung, Indonesia.
Arjuna Subject : Ilmu Pertanian dan Biologi (Semua) - Ilmu Pertanian dan Biologi (Lain-Lain)
Articles 2 Documents
 1 
Search results for , issue "Vol. 5 No. 2 (2023)" : 2 Documents clear
The In Silico Characterization of Lycopene Forming Phytoene Desaturase (CrtI) Protein from Wheat Leaf Rust Fungi (Puccinia triticina) Yehezkiel Vieri Polandos; Fenny Martha Dwivany; Karlia Meitha
3BIO: Journal of Biological Science, Technology and Management Vol. 5 No. 2 (2023)
Publisher : School of Life Sciences and Technology, Institut Teknologi Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5614/3bio.2023.5.2.1

Abstract

Carotenoid is a highly economical compound with a variety of bioactivities. However, 98% of total carotenoid used is still being manufactured by chemical-based synthesis, reducing bioactivities and is not environmentally friendly, hence the use of biofortification approach is sought.Lycopene forming phytoene desaturase (CrtI) is one of the key enzymes with the potential to develop as bioparts in recombinant carotenoid biosynthesis. CrtI from Puccinia triticina and Blakeslea trispora are considered as promising candidates due to the high amount of carotenoid inthe fungi. This research aims to characterize CrtI enzyme from P. triticina and B. trispora and the interaction with substrate, i.e.,15 cis-phytoene. The results showed that CrtI from P. triticina protein has 2 unique motifs, determining the three-dimensional CrtI protein structure. According to docking analysis, CrtI enzyme from P. triticina is predicted to bind to the substrate more spontaneously as indicated by the lower energy of affinity (-8.3 kcal mol-1) and more residues interaction compared to CrtI from Blakeslea trispora. In conclusion, the CrtI protein from P. triticina is suggested as the candidate for further exploration to design expression in a recombinant system.
The Structural Evaluations of SARS-CoV-2 Main Protease (Mpro): A Review for COVID-19 Antivirals Development Strategy Muhammad Hamzah Syaifullah Azmi; Ernawati Arifin Giri-Rachman
3BIO: Journal of Biological Science, Technology and Management Vol. 5 No. 2 (2023)
Publisher : School of Life Sciences and Technology, Institut Teknologi Bandung

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.5614/3bio.2023.5.2.2

Abstract

It has been almost four years since the first case of COVID-19 emerged, and the antivirals that could work specifically against SARS-CoV-2with a high efficacy are still under development. Main Protease (Mpro) of this virus plays a crucial role in virion maturation during itsreplication within the host cell. This protein works together with the papain-like protease (PLpro) to cleave polyprotein 1a  and 1ab  into a total of16 functional fragments of non-structural protein. Antiviral with the ability to inhibit the activity of Mpro could potentially prevent the virion replication, and they can be developed to target the catalytic or allosteric site of this protein. Antiviral that works on the catalytic site will act as competitive inhibitors of the substrate peptide which leads to the loss of Mpro function. Targeting the allosteric site (e.g. distal site and dimerization interface) will cause allosteric modu- lation of the protomer which could alter the protein 3D conformation and disrupt the formation of homodimer structure. This will affect the geometry and surface structure of the catalytic site which in turn decreases the affinity of the substrate peptide towards the Mpro catalytic site, resulting in a completeinactivation of the protein. Mutation study of Mpro amino acids sequence also reveals that the mutation frequency for each amino acid position isextremely low and negligible. Moreover, it is found that this protein has 24 mutational cold spot residues scattered within its structure which could be targeted for the development of antivirals due to its highly conserved nature.

Page 1 of 1 | Total Record : 2

 1 

Filter by Year

2023 2023


Reset
Filter By Issues
All Issue Vol. 7 No. 1 (2025): Vol. 7 No. 1 (2025) Vol. 7 No. 2 (2025) Vol. 6 No. 2 (2024) Vol. 6 No. 1 (2024) Vol. 5 No. 2 (2023) Vol. 5 No. 1 (2023) Vol. 4 No. 2 (2022) Vol. 4 No. 1 (2022) Vol. 3 No. 2 (2021) Vol. 3 No. 1 (2021) Vol. 2 No. 2 (2020) Vol. 2 No. 1 (2020) Vol. 1 No. 1 (2019) More Issue