1Department of Chemistry, Faculty of Science, Obafemi Awolowo University, Ile-Ife, Osun State, Nigeria
2Chemical Science Division, Saha Institute of Nuclear Physics, Kolkata, West Bengal, India
3Department of Chemistry, Faculty of Science, Tokyo University of Science, 1-3 Kagurazaka, Shinjuku-ku, Tokyo 162-8601, Japan
Journal of Polymer and Biopolymer Physics Chemistry.
2026,
Vol. 14 No. 1, 1-14
DOI: 10.12691/jpbpc-14-1-1
Copyright © 2026 Science and Education PublishingCite this paper: Temitayo O. Aiyelabola, Sayantan Pradhan, Takashiro Akitsu. Computational Evaluation of a Novel Nitrothiophene-Derived Schiff Base Ligand Against Breast Cancer-Associated Proteins and Andes Hantavirus Nucleoprotein: Molecular Docking and ADMET Analysis.
Journal of Polymer and Biopolymer Physics Chemistry. 2026; 14(1):1-14. doi: 10.12691/jpbpc-14-1-1.
Correspondence to: Sayantan Pradhan, Chemical Science Division, Saha Institute of Nuclear Physics, Kolkata, West Bengal, India. Email:
sayan23us@gmail.comAbstract
The identification of small molecules capable of interacting with multiple therapeutically relevant protein targets is an important strategy in early-stage drug discovery. In the present study, the Schiff base ligand ((N1E,N8E)-N1,N8-bis((5-nitrothiophen-2-yl)methylene)naphthalene-1,8-diamine; N1) was computationally evaluated against a panel of representative disease-associated proteins to investigate its target-binding profile. The primary focus was the assessment of N1 against breast cancer-associated receptor kinases, including EGFR, HER2, VEGFR2, and PI3K, which play central roles in oncogenic signaling pathways. In addition, the Andes hantavirus nucleoprotein was included as an exploratory antiviral target to examine the broader target recognition capability of the ligand rather than to propose a common therapeutic mechanism. Molecular docking studies were performed using AutoDock Vina with experimentally determined protein structures obtained from the Protein Data Bank. N1 demonstrated favorable binding affinities toward all investigated breast cancer targets, with docking scores of −8.708 kcal/mol for EGFR, −8.836 kcal/mol for HER2, −8.906 kcal/mol for VEGFR2, and −9.066 kcal/mol for PI3K. The ligand also exhibited a docking score of −8.8 kcal/mol against the Andes hantavirus nucleoprotein. Interaction analysis revealed multiple stabilizing hydrogen bonds, hydrophobic contacts, electrostatic interactions, and π-mediated interactions within the respective binding pockets.Drug-likeness assessment indicated compliance with Lipinski's and Ghose's rules, while ADMET prediction suggested favorable absorption and membrane permeability. Nevertheless, the predicted risks of hepatotoxicity, cardiotoxicity, and mutagenicity indicate that further structural optimization and experimental validation are required. Overall, this study demonstrates the potential of N1 as a promising scaffold for breast cancer-associated kinase inhibition while providing preliminary evidence of its broader protein-binding capability across biologically distinct targets.
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