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All Journal VALENSI Indonesian Journal of Biotechnology Science and Technology Indonesia Chimica et Natura Acta Indonesian Journal of Chemistry Communications in Science and Technology Chemistry Indonesian Journal of Chemical Research Jurnal Kartika Kimia Journal of Multidisciplinary Applied Natural Science Indonesian Chimica Letters
Hermawati, Elvira
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Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Chemical Engineering, Chemistry & Bioengineering Chemistry Education Energy Engineering Environmental Science Immunology & microbiology Materials Science & Nanotechnology Mathematics Physics

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Potential of Favipiravir Analogs as SARS-CoV-2 RdRp Inhibitors: Synthesis and In Silico Studies Alni, Anita; Lokitha, Angela; Maulana, Yusuf Eka; Hermawati, Elvira; Danova, Ade
Indonesian Journal of Chemistry Vol 26, No 1 (2026)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ijc.98538

Abstract

The novel severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is responsible for causing the lethal infectious disease known as COVID-19. The RNA-dependent RNA polymerase (RdRp) is a pivotal component that facilitates the translation of viral RNA into viral proteins. Therefore, our study aimed to synthesize new inhibitors from favipiravir (FVP) analogs by modifying the hydrophobicity through a nucleophilic aromatic substitution at the C-6 position of the pyrazine ring with alkoxy groups under acidic conditions. Moreover, the synthesized FVP analogs were investigated for their antiviral potency against SARS-CoV-2 RdRp through in silico studies. Five FVP analogs (3–7), including four known (3, 4, 5, 7) and one new (6), were successfully synthesized with yields ranging from 2.3 to 32.7%. All favipiravir analogs could be drug-likeness with inactive hepatotoxicity and carcinogenicity. The docking study showed that compound 5 exhibited a strong binding affinity with a binding score of −7.00 kcal/mol by interacting with the catalytic site residues of Asp618 and Asp760 of SARS-CoV-2 RdRp. Furthermore, the molecular dynamics simulation revealed that the compound 5 was stable, as indicated by RMSD, Rg, solute H-bonds, RMSF, and binding energy calculations. Thus, these results suggest that the FVP-RTP analog (5) may have antiviral potency by targeting SARS-CoV-2 RdRp.
New Pyrrole-Chalcone Hybrids Against Acetylcholinesterase: Synthesis, In Vitro, and Computational Studies Ridwanuloh, Dadan; Danova, Ade; Hermawati, Elvira; Chavasiri, Warinthorn; Ihsanawati, Ihsanawati; Alni, Anita
Journal of Multidisciplinary Applied Natural Science Articles in Press
Publisher : Pandawa Institute

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.47352/jmans.2774-3047.375

Abstract

Acetylcholinesterase (AChE) inhibition remains a central therapeutic approach for Alzheimer’s disease (AD), as it helps preserve synaptic acetylcholine levels, enhances cholinergic neurotransmission, and mitigates early cognitive decline. In this study, eight novel pyrrole–chalcone hybrids (3–10), consisting of four pyrrole–chalcones (3–6) and four pyrrole–chalcone amides (7–10), were designed, synthesized, and biologically evaluated for AChE inhibition. Among them, compound 8 (N-(4-methoxybenzyl)-pyrrole–chalcone amide) and compound 10 (N-(3,4-dimethoxybenzyl)-pyrrole–chalcone amide) demonstrated the strongest inhibitory activity, with IC₅₀ values of 3.1 and 2.8 µM, respectively, comparable to galantamine. Kinetic assays confirmed that both compounds act as noncompetitive inhibitors, as indicated by reduced Vmax without significant alteration in Km, while compound 10 exhibited Ki of 0.8 µM, reflecting high enzyme affinity. Molecular docking revealed strong binding interactions of compounds 8 and 10 with key AChE residues (Trp84, Phe330, Tyr334), supported by π–π stacking, π–alkyl interactions, and hydrogen bonding, with binding energies of –9.2 (compound 8) and –8.9 kcal/mol (compound 10). Molecular dynamics simulations further demonstrated that compound 10 forms a more stable and compact complex with AChE, as indicated by consistent RMSD values and a stable radius of gyration. SwissADME analysis confirmed favorable pharmacokinetic profiles for both ligands, including Lipinski compliance, high GI absorption, and absence of PAINS alerts, despite the lack of predicted BBB permeability. Overall, compound 10 emerges as the most promising noncompetitive AChE inhibitor in this series, exhibiting strong binding affinity, structural stability, and drug-likeness, thus warranting further optimization and in vivo evaluation.
Co-Authors Ade Danova Anita Alni, Anita Aqilah, Amadita Shafa Chavasiri, Warinthorn Danova, Ade Darmayani, Ni Komang Tri Didin Mujahidin Emmy Yuanita IHSANAWATI IHSANAWATI Ika Oktavianawati Iqbal Musthapa Kartika, Irma Ratna Kurniadewi, Fera Lokitha, Angela Maria Ulfa Maulana, Yusuf Eka Muhammad Reza Muktiningsih Nurjayadi Ridwanuloh, Dadan Risma, Melania Roswanda, Robby Sa'adah, Pipih Lutfi Sudirman Sudirman Surya Hadi Tri Dharmayani, Ni Komang Wahidatun, Wahidatun Wonganan, Piyanuch Yulvia, Ana