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All Journal Fullerene Journal of Chemistry Jurna Beta Kimia
Najoan, Jessika Maya Jovanka
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Chemical Engineering, Chemistry & Bioengineering Chemistry Education

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Molecular Docking Of Cyclosenegalin A As Anticancer Paat, Vlagia Indira; Aloanis, Anderson Arnold; Najoan, Jessika Maya Jovanka
Jurnal Kimia Fullerene Vol 10 No 1 (2025): Fullerene Journal Of Chemistry
Publisher : Fakultas Matematika dan Ilmu Pengetahuan Alam

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.37033/fjc.v10i1.713

Abstract

Cancer is recognized as a leading cause of death globally, responsible for approximately 14.5% of all deaths,. Cyclosenegalin A showed activity against DU-145 human prostate cancer cell line with IC50 of54.92.35μM. This study aims to investigate whether the cyclosenegalin A compound can interact with the target receptors 4IEH and potentially act as an anticancer candidate. The results of the study show that the docking of cyclosenegalin A with the 4IEH receptor yielded the best results, with an affinity value of -8.88 kcal/mol. The hydrogen bonding at the GLY 104, ASP 70, VAL 92, and GLU 95 amino acids was identical to that observed in the standard ligand, n-heteroarilsulfonamides. The interaction between cyclosenegalin A and the target receptor is effective, indicating that cyclosenegalin A holds potential as an anti-cancer candidate.
In Silico Study of the YAKRCFR Peptide Structure and Its Interaction with Human Peroxiredoxin-5 Najoan, Jessika Maya Jovanka; Rumampuk, Rymond Jusuf; Paat, Vlagia Indira; Aloanis, Anderson Arnold
Jurnal Beta Kimia Vol 5 No 2 (2025): Volume 5 Number 2, November 2025
Publisher : Universitas Nusa Cendana

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35508/jbk.v5i2.22710

Abstract

The identification of bioactive peptides with therapeutic potential is an emerging focus in drug discovery. In this study, we evaluated the structural stability and binding affinity of the oyster-derived peptide YAKRCFR through molecular modeling and docking simulations against the human peroxiredoxin receptor. Structural prediction using the PEP-FOLD4 server revealed a consistent α-helical conformation across all models, stabilized by key intramolecular hydrogen bonds and favorable sOPEP energy values. Molecular docking was validated with a root mean square deviation (RMSD) of 0.273 Å, confirming the reliability of the docking protocol. The YAKRCFR peptide exhibited a strong binding affinity with the 1HD2 receptor (ΔG = –8.1 kcal/mol), outperforming both ascorbic acid (–6.1 kcal/mol) and the native ligand (–4.862 kcal/mol). Detailed interaction analysis indicated that YAKRCFR forms stable hydrogen bonds and van der Waals interactions with critical residues such as ILE A119 and PHE A120, contributing to its thermodynamic stability and binding specificity. These findings suggest that YAKRCFR holds promise as a lead compound for further development in peptide-based therapeutic strategies, particularly for targets involving the human peroxiredoxin receptor.
Co-Authors Anderson Arnold Aloanis Paat, Vlagia Indira Rymond Jusuf Rumampuk