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All Journal Indonesian Journal of Biotechnology Science and Technology Indonesia Communications in Science and Technology Chemistry Indonesian Journal of Chemical Research Jurnal Kartika Kimia
Chavasiri, Warinthorn
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Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Education Engineering Environmental Science Immunology & microbiology Materials Science & Nanotechnology Physics

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Synthesis and Biological Evaluation of N'-Arylidene-4-Hydroxybenzohydrazides against α-Glucosidase Enzyme Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn
Jurnal Kartika Kimia Vol 6 No 2 (2023): Jurnal Kartika Kimia
Publisher : Department of Chemistry, Faculty of Sciences and Informatics, University of Jenderal Achmad Yani

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.26874/jkk.v6i2.210

Abstract

Hydrazides have been reported to have a broad spectrum of bioactivities, such as anticancer, antifungal, antibacterial, and antidiabetic. Thus, our work aimed to synthesize N'-arylidene-4-hydroxybenzohydrazides and investigate their α-glucosidase inhibition. Three compounds (AD-H1-3) were synthesized with a yield of product from 33 to 65% and then characterized using 1H-and 13C-NMR spectroscopy. The in vitro α-glucosidase inhibition demonstrated that AD-H2 possessing two hydroxy groups on arylidene moiety showed the best inhibitory activity against α-glucosidase enzyme with an IC50 value of 14.4 µM compared with acarbose as a positive control with IC50 value of 93.6 µM. Thus, AD-H2 could be a candidate as a lead compound for antidiabetics.
Synthesis, Evaluation, and Molecular Docking Study of 4-Monoacyl Resorcinol Against Tyrosinase Enzyme Danova, Ade; Maulana, Yusuf Eka; Hermawati, Elvira; Chavasiri, Warinthorn
Indonesian Journal of Chemical Research Vol 11 No 2 (2023): Edition for September 2023
Publisher : Jurusan Kimia, Fakultas Matematika dan Ilmu Pengetahuan Alam, Universitas Pattimura

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.30598//ijcr.2023.11-nov

Abstract

Tyrosinase is a crucial enzyme in melanin production to protect the skin from ultraviolet, leading to skin cancers. This study synthesized eight compounds of acyl resorcinol with long-chain carbon (1-8) and structurally elucidated by 1H and 13C NMR. The in vitro evaluation of eight synthesized compounds against tyrosinase enzyme showed that 4-heptanoyl resorcinol (6) exhibited high inhibitory activity compared with the kojic acid as standard. In addition, the molecular docking study demonstrated that 6 showed lower binding energy (-7.3 kcal/mol) than kojic acid (-6.9 kcal/mol) and possessed interaction with crucial residues in the active site.
Discovery of thymol-fused chalcones as new competitive \(\alpha\)-glucosidase inhibitors: Design, synthesis, biological evaluation, and molecular modeling studies Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn; Mujahidin, Didin; Alni, Anita; Roswanda, Robby
Communications in Science and Technology Vol 9 No 2 (2024)
Publisher : Komunitas Ilmuwan dan Profesional Muslim Indonesia

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21924/cst.9.2.2024.1497

Abstract

This study aims to synthesize and evaluate the inhibitory activity of thymol derivatives targeting ?-glucosidase using in vitro and in silico studies. Ten thymol derivatives (2-11) including five new thymol-fused chalcones (7-11) were successfully synthesized. Among them, four compounds (4, 8, 9, 11) showed the best inhibitory activity with IC50 values of 18.45, 13.75, 8.86, and 10.67µM compared with acarbose (IC50 = 832.82 µM), respectively. The kinetic study of three new thymol-fused chalcones (8, 9, 11) exhibited a competitive inhibition. Molecular docking demonstrated the predicted interactions between ligand (8, 9, 11) and ?-glucosidase, which are responsible for inhibiting the enzyme's catalytic abilities. Furthermore, molecular dynamics simulation of the enzyme-ligand 9 complex indicated that this complex was stable in aqueous condition. This research contributes significantly to the understanding of thymol-fused chalcones that may have therapeutic potential and their possible application in the treatment of type 2 diabetes mellitus (T2DM) for further study.
In vitro evaluation, molecular docking, and molecular dynamics studies of resorcinol derivatives against yeast α‐glucosidase Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn; Mujahidin, Didin; Musthapa, Iqbal; Kurniadewi, Fera
Indonesian Journal of Biotechnology Vol 30, No 3 (2025)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijbiotech.106495

Abstract

Nine resorcinol derivatives were evaluated for their ability to inhibit yeast α‐glucosidase using the in vitro method. Three molecular docking programs (Autodock Vina, Autodock4 and DockThor) were employed to determine the binding energies. The results showed that two resorcinol derivatives possessing butanoyl (1) and butyl (9) groups demonstrated good inhibitory activity against α‐glucosidase, with IC50 values of 75.9 and 33.3 µM respectively, compared with other derivatives (2–8) and acarbose (IC50 = 832.8 µM). Furthermore, molecular docking indicated that compounds 1 and 9 had better binding affinities than acarbose and the native ligand. Both compounds showed similar interactions with Asp349 and Glu408, which were associated with acarbose and the native ligand. Moreover, molecular dynamics analysis indicated that compound 9 exhibited greater stability than compound 1 when complexed with α‐glucosidase. Therefore, compound 9 has the potential for further studies, both in vitro and in vivo, to evaluate its toxicity, side effects and efficacy.
Anti-tyrosinase Activity of 3’,4’,5’-Trimethoxychalcones: Experimental and Computational Studies Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn; Mujahidin, Didin; Musthapa, Iqbal; Kurniadewi, Fera
Science and Technology Indonesia Vol. 10 No. 4 (2025): October
Publisher : Research Center of Inorganic Materials and Coordination Complexes, FMIPA Universitas Sriwijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.26554/sti.2025.10.4.982-989

Abstract

Tyrosinase inhibitors are utilized as preservatives in the food industry and skin-lightening agents in the medical and cosmetic sectors. However, there has been little progress in clinical trials owing to challenges such as low bioavailability, significant skin irritation, and instability. Hence, the objective of this study was to evaluate the inhibitory activity of 3’,4’,5’-trimethoxychalcones through in vitro, molecular docking and molecular dynamics studies targeting tyrosinase. Five 3’,4’,5’-trimethoxychalcones (1-5) were evaluated their biological activity against tyrosinase for the first time. Compounds 4 and 5 were excellent inhibitory activity against tyrosinase with IC50 values of 1.9 and 1.7 μm compared with kojic acid and ascorbic acid. Isovanillin and catechol moieties are vital in this present study. This result was supported with molecular docking by shaping interaction in the catalytic site with histidine residues and the stability evaluation of the inhibitor-protein complexes using molecular dynamics simulation. The lipinski’s rules showed a fit with two potential inhibitors (4, 5). Therefore, 3’,4’,5’-trimethoxychalcones possessing isovanillin and catechol parts in the B ring are promising candidate for further study as tyrosinase inhibitors by evaluating their efficacy in vitro and in vivo.
Co-Authors Ade Danova Anita Alni, Anita Didin Mujahidin Hermawati, Elvira Iqbal Musthapa Kurniadewi, Fera Maulana, Yusuf Eka Roswanda, Robby