Article Per Year (5 Year)
p-Index From 2020 - 2025
0
P-Index
This Author published in this journals
All Journal HAYATI Journal of Biosciences Annales Bogorienses
Hariyatun, Hariyatun
Unknown Affiliation
Agriculture, Biological Sciences & Forestry Earth & Planetary Sciences

Published : 2 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 2 Documents
Search

 1 
Evaluation of Curcumin-derived Carbon-dots' Inhibitory Activity as SARS-CoV-2 Antiviral Candidate Using Chemical Crosslinking Taharuddin, Audrey Angelina Putri; Yamahoki, Nicholas; Stephanie, Rebecca; Agustiyanti, Dian Fitria; Wisnuwardhani, Popi Hadi; Angelina, Marissa; Rubiyana, Yana; Ningrum, Ratih Asmana; Wardiana, Andri; Desriani, Desriani; Hariyatun, Hariyatun; Iskandar, Ferry; Permatasari, Fitri Aulia; Giri-Rachman, Ernawati Arifin; Fibriani, Azzania
HAYATI Journal of Biosciences Vol. 33 No. 1 (2026): January 2026
Publisher : Bogor Agricultural University, Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.4308/hjb.33.1.232-239

Abstract

In our previous work, we demonstrated that curcumin-derived carbon dots (Cur-CDs) have potential as antivirals for COVID-19. However, the precise mechanism of action remains unclear. This study investigated the potential of Cur-CDs against SARS-CoV-2 by targeting the dimerization of the C-terminal domain of nucleocapsid protein (N-CTD) using chemical crosslinking. Recombinant SARS-CoV-2 N-CTD was expressed, purified, and subjected to chemical crosslinking. The dimerization inhibition ability of Cur-CDs was assessed with ligand concentrations ranging from 0 to 2,000 μg/mL. Successful inhibition —defined as a noticeable reduction in SARS-CoV-2 N-CTD dimer band intensity on SDS-PAGE—was observed when Cur-CDs were present at 8 to 16 times the protein concentration. We hypothesize that Cur-CDs bind to the dimerization residues, preventing non-covalent interactions between monomers and limiting dimer formation. Our findings suggest that Cur-CDs could be a promising antiviral strategy for SARS-CoV-2, especially targeting the dimerization of the nucleocapsid protein. Additionally, this study also highlights the use of chemical crosslinking as a valuable tool for interaction-based drug screening.
Expression of An Immunogenic Intimin Fragment of EHEC O157:H7 in Escherichia coli Periplasm under The Control of A Rhamnose-Based Regulated Promoter Hariyatun, Hariyatun; Suwanto, Antonius; Kusharyoto, Wien
Annales Bogorienses Vol. 18 No. 1 (2014): Annales Bogorienses
Publisher : BRIN

Show Abstract | Download Original | Original Source | Check in Google Scholar

Abstract

Intimin is the main adhesin of Enterohemorrhagic E. coli (EHEC) O157:H7 bacteria which are the most common leading infectious cause of bloody diarrhea and acute kidney failure in children who develop hemolytic uremic syndrome (HUS). Intimin is required for persistent bacterial colonization to eukaryotic host cell and its receptor-binding activity is localized at the C-terminus 282 amino acids (Intimin282). Thus, Intimin282 is an attractive antigen candidate that could be useful in vaccine and diagnostic systems against EHEC infections. Previous studies had reported expression of Intimin in E. coli cytoplasm using commonly used prokaryotic expression systems. However, it usually encountered several problems, i.e. low expression level, leaky expression, inclusion body formation, and truncated protein. The pRHA vector, which is tightly regulated by Lrhamnose and D-glucose, represents a viable alternative E. coli expression system to overcome such problems. Moreover, E. coli periplasm has an advantage of maintaining protein functionality by providing an oxidative environment that is more efficient than cytoplasm. However, to date there is no study about Intimin expressionusing pRHA expression system and/or in E. coli periplasm. Accordingly, we constructed a recombinant pRHA vector harbouring the respective gene to investigate the expression of an immunogenic Intimin fragment of EHEC O157:H7 in E. coli periplasm. The gene encoding His6-tagged Intimin282 (Int282) together with pelB signal sequence was cloned into the pRHA vector, subsequently expressed in E. coli JM109 and purified. Expression and purification of Int282 were verified by SDS-PAGE and Western blot. The result showed that Int282 was successfully expressed in E. coli periplasm with a protein size of approximately 32 kDa, which corresponded with the predicted size of the protein based on its amino acid sequence.
Co-Authors Agustiyanti, Dian Fitria Andri Wardiana, Andri Antonius Suwanto Desriani Desriani ERNAWATI ARIFIN GIRI-RACHMAN Ferry Iskandar Fibriani, Azzania Kusharyoto, Wien Marissa Angelina Permatasari, Fitri Aulia Popi Hadi Wisnuwardhani, Popi Hadi RATIH ASMANA NINGRUM Stephanie, Rebecca Taharuddin, Audrey Angelina Putri Yamahoki, Nicholas Yana Rubiyana, Yana