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All Journal VALENSI Current Biochemistry Borneo Journal of Pharmacy
Irsal, Riyan Alifbi Putera
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Biochemistry, Genetics & Molecular Biology Chemistry Education Medicine & Pharmacology

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Flavonoid Concentration and Tyrosinase Inhibition Activity of Ethanol Extract of Piper crocatum (Piper crocatum var. Ruiz & Pav) from Various Regions in Indonesia and Their Correlations Irsal, Riyan Alifbi Putera; Safithri, Mega; Andrianto, Dimas; Mardliyati, Etik
Jurnal Kimia Valensi Jurnal Kimia VALENSI Volume 9, No. 1, May 2023
Publisher : Syarif Hidayatullah State Islamic University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.15408/jkv.v9i1.31426

Abstract

Hyperpigmentation is a condition of darkening of the skin which is generally caused by an increase in melanin production. Melanin is produced in melanocytes by the enzyme tyrosinase. Piper crocatum contains flavonoid compounds that are known from previous research to inhibit tyrosinase. The goals of this study were to determine the tyrosinase inhibitory activity and total flavonoid content of seven accessions, as well as look at the Pearson’s correlation and clustering PCA (principal component analysis). The method used was water content analysis, extraction yield measurement, total flavonoids analysis, and in vitro tyrosinase inhibition. Based on the results, P. crocatum from Kendari had the best yield and total flavonoid content of 24.07% and 5.10 mg QE g-1, while P. crocatum from Bogor had the lowest water content with a value of 6.21% and the best in tyrosinase inhibition of 13.77. The correlation between total flavonoid content and percent inhibition showed a very weak correlation. The results of clustering formed four clusters of seven accessions based on total flavonoids and percent inhibition. The cluster was divided into Malang (506mDPL) and Jayapura (287mDPL), Banda Aceh (0.80mDPL) and Bandung (670mDPL), Samarinda (8mDPL) and Bogor (190-350m DPL), and Kendari (14mDPL). In conclusion, the correlation between total flavonoid levels and percent inhibition is very weak and regional diversity had a significant effect on total flavonoids and total inhibition.
Molecular Docking and Dynamics of Xylocarpus granatum as A Potential Parkinson’s Drug Targeting Multiple Enzymes Irsal, Riyan Alifbi Putera; Gholam, Gusnia Meilin; Firdaus, Dzikri Anfasa; Liwanda, Novian; Chairunisa, Fernanda
Borneo Journal of Pharmacy Vol. 7 No. 2 (2024): Borneo Journal of Pharmacy
Publisher : Institute for Research and Community Services Universitas Muhammadiyah Palangkaraya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.33084/bjop.v7i2.6810

Abstract

Parkinson's disease is a global health challenge affecting over 10 million individuals worldwide, leading to increased disability-adjusted life years (DALYs) and a rise in mortality rates. This study explores the potential anti-Parkinson's properties of Xylocarpus granatum, focusing on its interaction with key enzymes associated with the disease: catechol-O-methyltransferase (COMT), adenosine A2A receptor (A2AR), and monoamine oxidase-B (MAO-B). Using molecular docking and molecular dynamics approaches with YASARA Structure, the ethanol extract of X. granatum was investigated for its mechanism of action. Among 30 compounds, five demonstrated promising binding affinities. Structural flexibility analysis revealed minimal fluctuations in active-site residues, highlighting the stability of key complexes involving kaempferol, epicatechin, epigallocatechin, and native ligands. Molecular Mechanics Poisson–Boltzmann Surface Area (MM-PBSA) simulations provided insights into the binding energy of these complexes. Notably, kaempferol exhibited higher binding energy than the natural ligand, suggesting superior binding affinity. Analysis of the average radius of gyration (Rg) showcased control drug-MAO-B exhibited higher Rg values, indicating a more flexible protein conformation. Confirming mode stability with root mean square deviation (RMSD) analysis shows overall stability, except in the A2AR-bound complex. The study's collective findings underscore the structural stabilization of ligand-protein complexes, contributing valuable insights into the potential anti-Parkinson's properties of X. granatum. These discoveries hold promise for developing more effective therapies for Parkinson's disease and significantly contribute to the neurology field.
Molecular docking: Bioactive compounds of Mimosa pudica as an inhibitor of Candida albicans Sap 3 Gholam, Gusnia Meilin; Firdausy, Iman Akhyar; Artika, I Made; Abdillah, Ramadhani Malik; Firmansyah, Ridwan Putra; Irsal, Riyan Alifbi Putera; Zahra, Hafizh
Current Biochemistry Vol. 10 No. 1 (2023)
Publisher : IPB University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.29244/cb.10.1.4

Abstract

Candida albicans (C. albicans) is a commensal microbiota that resides in humans. However, in certain cases, C. albicans can infect and cause several diseases to humans. This study aimed to investigate the interaction between Mimosa pudica bioactive compounds and C. albicans Sap 3. Molecular docking analysis was carried out using YASARA structure. The procedures involved preparation of ligands and target receptor, molecular docking, data analysis and visualization. All 3D ligands were downloaded from PubChem NCBI, while target receptor was downloaded from RCSB PDB. The interaction between Mimosa pudica bioactive compounds against Sap 3 resulted in a binding energies ranges from 5,168 – 7,480 kcal/mol and most of the interactions formed were relatively strong. Furthermore, the test ligands had contact with the catalytic residues and substrate binding site pockets S1/S2/S3/S4 on the target receptor. Bioactive compounds of Mimosa pudica have relatively good interactions in inhibiting C. albicans Sap 3
Co-Authors Abdillah, Ramadhani Malik Chairunisa, Fernanda DIMAS ANDRIANTO Etik Mardliyati, Etik Firdaus, Dzikri Anfasa Firdausy, Iman Akhyar Firmansyah, Ridwan Putra Gholam, Gusnia Meilin I MADE ARTIKA Liwanda, Novian Mega Safithri Zahra, Hafizh