Emodin (1,3,8-trihydroxy-6-methyl-9,10-anthraquinone) is an anthraquinone bioactive compound used as a lead compound because it exhibits potential anticancer properties. Structural modifications were made at the C3 position and its relationship to cytotoxic activity against the HepG2 cell line to determine the pharmacophore group of this compound. The hydroxy group at C3 emodin is converted to an ester group to produce 3-acetyl emodin. In addition, docking simulations into the cancer target protein casein kinase-2 were also carried out to predict molecular interactions. Emodin was reacted with anhydrous acetate and confirmed the product confirmation using LCMS/MS, FTIR, 1H-NMR, and 13C-NMR. Emodin and 3-acetyl emodin were tested for cytotoxicity against HepG2 cells in vitro. Cytotoxic emodin and 3-acetyl emodin tests on HepG2 cells resulted in Cytotoxic concentrations 50 (CC50) of 0.54 mM and 0.42 mM, respectively. The results showed that modifying the C3 hydroxyl group with acetyl can increase the cytotoxic effect more than emodin. This research is expected to provide information regarding the structure-activity relationship of emodin in cancer cells and the expansion of new drug applications for additional cancers.
Depleting collagen in the skin due to the appearance of the collagenase enzyme is one of the causes of aging. The objective of this study was to predict the effectiveness of some bioactive compounds found in the leaves of Murraya paniculata, known as Kemuning in Indonesia, by molecular docking as a potential inhibitor for the collagenase enzyme by analyzing the Binding Energy and the potential interaction between ligan and macromolecule as well as an antioxidant investigation by DPPH method. According to several studies, more than a hundred small molecules are contained in M. paniculata, and all of the ligands will be tested in-silico using AutoDock computational software. In contrast, Pymol and Discovery Studio were used for visualization. The research phase begins with ligand and macromolecule preparation, followed by grid box determination and AutoDock, analyzing the docking score and visualizing the dock conformations. Of all the ligands tested, 50 compounds had the potential to inhibit the performance of the collagenase enzyme with a binding affinity lower than −7 kcal/mol compared to Gallic Acid and Ascorbic acid. Compound noracronycine has the best binding affinity by −9.35 kcal/mol, while the compound with the lowest value is germacrene d by −7.06 kcal/mol. However, Diphenylpicrylhydrazyl (DPPH) testing method used in this study revealed that the antioxidant capacity (IC 50 ) of the plant extracted with methanol was 2,360.73 ppm, which was significantly different from that of the positive control. Since the large number of compounds that play a role in inhibiting the development of the collagenase enzyme from this plant exist, there is an opportunity to be used as raw material for cosmetics and nutraceuticals.
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