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The Cytotoxicity of Agaro-Oligosaccharides and Neoagaro-Oligosaccharides on Macrophage Cells Pratitis, Visi Endah; Puspitasari, Pinki Anggrahini; Hanbal, Mayland Muhammad; Tsabitah, Khansa; Juliadmi, Dian; Saksono, Budi; Wijayanti, Nastiti
Mutiara Medika: Jurnal Kedokteran dan Kesehatan Vol 24, No 2 (2024): July
Publisher : Universitas Muhammadiyah Yogyakarta

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.18196/mmjkk.v24i2.21059

Abstract

Agarose is a polysaccharide from red algae. Enzymatic hydrolysis of agarose can produce Agaro-Oligosaccharidess (AOS) and Neoagaro-Oligosaccharidess (NAOS). Different times of enzymatic hydrolysis can produce different types of AOS and NAOS based on their degree of polymerization (DPs). This study aims to examine the cytotoxicity of AOS and NAOS with different hydrolysis times on the macrophage cell line RAW 264.7. The parameters used were the percentage of cell viability and IC50 value. The cytotoxicity test using MTT assay and One-way ANOVA were used as statistical tests. The results showed that AOS-0 at a concentration below 125 µg/mL was not toxic and showed moderate toxicity up to a high concentration of 1000 µg/mL, while AOS hydrolyzed for 24 h (AOS-24) was not toxic to RAW 264.7 cells at all concentrations tested. The different results were shown in all NAOS samples, which were highly toxic to RAW 264.7 cells in the 125 to 1000 µg/mL, indicating that it was concentration dependent. The results showed that different hydrolysis times caused differences in the structure of AOS and NAOS compounds and influenced the toxicity level. Research development for further studies on antioxidants and anti-inflammatory needs more attention to the sample type and hydrolysis time.
Inositol Hexakisphosphate (InsP₆) Induces Apoptosis via Caspase-Dependent Pathways: Molecular Docking Insights Sandra, Ferry; Ranggaini, Dewi; Halim, Johni; Pakpahan, Alfred; Pratitis, Visi Endah; Lee, Kyung Hoon
The Indonesian Biomedical Journal Vol 17, No 5 (2025)
Publisher : The Prodia Education and Research Institute (PERI)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.18585/inabj.v17i5.3810

Abstract

BACKGROUND: Inositol hexakisphosphate (InsP₆) exhibits anticancer activity, especially by inducing intrinsic and extrinsic apoptotic pathways. However, there is still no molecular docking evidence that directly examines InsP₆ interactions with either upstream or downstream apoptotic regulators. Therefore, the current study was conducted to investigate the molecular docking of InsP₆ to caspases as upstream/downstream apoptotic regulators.METHODS: Ligands including InsP₆, InsP₅, InsP₄, histone deacetylase inhibitor, and caspase inhibitors were retrieved from PubChem, while target proteins (histone, caspase-8, caspase-2, and caspase-3) were obtained from the Protein Data Bank. Ligand toxicity was predicted using ProTox-3.0, and physicochemical properties were analyzed with SwissADME. Ligand structures were energy-minimized using PyRx with the Universal Force Field, while proteins were prepared by removing water molecules and non-essential heteroatoms in BIOVIA Discovery Studio. Molecular docking was conducted using CB-Dock 2.0, with binding poses selected based on the lowest Vina score, and ligand–protein interactions were visualized in Discovery Studio.RESULTS: Molecular docking results showed that InsP₆ bound strongly to histone, caspase-8, caspase-2, and caspase-3 with affinities comparable to reference inhibitors, forming multiple hydrogen bonds with key active-site residues. InsP₆, InsP₅, and InsP₄ exhibited several similar binding sites to caspase-3, with only minor differences in binding affinity.CONCLUSION: InsP₆ shows strong binding to histone, caspase-8, caspase-2, and caspase-3 based on in silico results, supporting its role in inducing both extrinsic and intrinsic apoptotic pathways. Taken together, InsP₆ could be a potential inducer of apoptosis in cancer cells.KEYWORDS: cancer, apoptosis, InsP₆, InsP₅, InsP₄, caspase, in silico, molecular docking