Spectroscopic characterization and geometry optimization of a ruthenium(II) complex with a limonene-derived amino-oxime ligand: DFT/TD-DFT inspection, in silico molecular docking, and dynamics simulations for a potent cancer drug.

Authors

Mohamed El Hllafi, Anas Chraka, Yousra El Fannassi, Yosra Benabdelouahab, Mounir Nechar, Abdelaziz Dahdouh, Mohamed Amin El Amrani

Published in

Journal of computer-aided molecular design. Volume 40. Issue 1. Jun 19, 2026. Epub Jun 19, 2026.

Abstract

In this paper, we investigated the structure of a ruthenium(II) complex bearing a limonene-derived amino-oxime ligand using UV-Vis and FT-IR spectroscopy. The compound exhibited potent anticancer activity, with IC₅₀ values up to 12 times lower than those of cisplatin against PC-3 (prostate), A-549 (lung), and HeLa (cervical) cancer cell lines. Density Functional Theory (DFT) and Time-Dependent Density Functional Theory (TD-DFT) calculations were performed using the B3LYP and PBE0 hybrid functionals. The theoretical results were compared with the experimental data, and the optimized molecular geometry, along with the simulated UV-Vis and FT-IR spectra, showed excellent agreement with the experimental observations. Notably, the PBE0 functional demonstrated slightly better consistency, highlighting its suitability for modelling the structural and spectroscopic properties of the complex. Further analyses were carried out to elucidate the electronic structure and reactivity of the Ru(II) complex, including global reactivity descriptors, frontier molecular orbital (FMO) analysis, Mulliken charge distribution, and molecular electrostatic potential (MEP) mapping, as well as electron localization function (ELF) and localized orbital locator (LOL) analyses. Molecular modelling studies were also conducted to investigate the interaction between the Ru(II) complex and human serum albumin (HSA). Molecular docking, performed through 100 independent runs, revealed two representative binding poses within the principal drug-binding cavity, selected from the dominant (63%) and secondary (34%) clusters. To evaluate the stability of these binding modes, 100 ns molecular dynamics (MD) simulations were carried out. Both poses exhibited stable interaction patterns, confirming the consistent binding of the Ru(II) complex to HSA. Overall, the computational findings are in strong agreement with the experimental data, supporting the proposed binding mechanism and further highlighting the therapeutic potential of this ruthenium-based complex as a promising anticancer candidate.

PMID:
42315715
Bibliographic data and abstract were imported from PubMed on 19 Jun 2026.

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