Onchidiid slug (Onchidium typhae) is a nudibranch that coastal communities in West Kalimantan have widely used as wounds. The study aims to characterize the West Kalimantan water O. typhae as antibacterial and antifungal. The study of O. typhae was carried out in several stages: preparation and optimization, extraction by Quinn method, characterization and identification of bioactive compounds, and antibacterial and antifungal assay using the microdilution method. The result of the proximate test showed that O. typhae powder contains high protein, namely 67.68%. Phytochemical screening results from methanol, ethyl acetate, and chloroform extracts contain alkaloids and amino acids. Methanol, chloroform, and ethyl acetate extract 1% of O. typhae showed inhibitory activity against Staphylococcus aureus, Escherichia coli, and Candida albicans. The most significant inhibition value was indicated by chloroform extract 1%, where the inhibition value against S. aureus, E. coli, and C. albicans was 82±0.01%; 85.8±0.01%; 85±0.01%, respectively. From these results, O. typhae powder can be developed as a wound medicine through its antibacterial and antifungal activity.
Alpha (a) and beta (β) asarone were identified as the main compounds of red Jeringau (Acorus calamus L.) and had antimicrobial properties. This study aimed to know these two compounds' antibacterial mechanism and toxicity prediction against the PBP 2 protein and 50S Ribosomal Protein of Shigella flexneri. Molecular docking protocol using PyRx device was performed with Exhaustiveness value= 106, grid x=38.738375, y=112.645792, z=46.926417 for PBP2, and grid x=71.721251, y=47.551601, z=9.663173 for 50S Ribosomal Protein. The molecular docking results on the α -Asarone compound obtained an affinity value of -5.7 kcal/mol for PBP2 and an affinity value of -5.6 kcal/mol for 50S Ribosomal Protein. In comparison, β-Asarone had an affinity value of -5.6 kcal/mol to PBP2 and an affinity value of -5.7 kcal/mol for 50S Ribosomal Protein. The α and β-Asarone affinity had better values than the control. Molecular docking of α and β-Asarone compounds results in ionic bonds to the TYR529 amino acid and polar bonds to the ASN552 amino acid of PBP2. However, only β-Asarone produces ionic bonds at the amino acid ILE17 and polar bonds at GLU13 from 50S Ribosomal Protein. Based on this study, the α and β-Asarone compounds were shown to have antibacterial activity by interfering with the permeability of the bacterial cell wall. Both compounds are also predicted to have carcinogenic and mutagen effects.
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