Ni(II), Pd(II) and Pt(II) complexes with SNO-group thiosemicarbazone and DMSO: Synthesis, characterization, DFT, molecular docking and cytotoxicity.

• Square planar complexes of Ni2+, Pd2+ and Pt2+ with thiosemicarbazone (SNO) ligand. • DMSO coordinate via S to Pd(II) and Pt(II) complexes and X-ray crystal structure. • 3D geometry optimization was investigated using DFT approach. • Molecular docking against tyrosine kinase domain of the EGFR (1M17) was performed. • Cytotoxicity against Hela cancer and normal endothelial human cell lines (Eahy926). The ligand H 2 L with SNO sites and DMSO coordinated to Pd(II) and Pt(II) form square planar [PdL.dmso] and [PtL.dmso] complexes, whereas the Na[NiL.OAc] form with same ligand and CH 3 COO−. FTIR, UV-Vis, and 1H and 13C NMR spectroscopy and micro and physical analysis were used to characterize the compounds. The structures of [PdL.dmso] and [PtL.dmso] complexes were completely elucidated with single crystal X-ray diffraction analysis. The 6–311 G (d, p) and LANL2DZ basis sets of density functional theory (DFT) with the B3LYP approach were utilized to determine the optimal molecular geometries of compounds as well as the HOMO-LUMO energies and other metrics. The [PdL.dmso] showed the highest activity among all the compounds, with an IC 50 of 15.6 µM and a selectivity index (SI) of 2.8 against Hela. The complexes Na[NiL.OAc] and [PtL.dmso] exhibited significant activity against Hela with IC 50 of 105.7 µM and IC 50 of 166 µM respectively, whereas the ligand showed very poor activity. The complexes [PdL.dmso], [PtL.dmso] and ligand, H 2 L exhibited moderate activity against normal Eahy926 with IC 50 values of 43.3 µM, 45 µM, and 185 µM, respectively whereas, the Na[NiL.OAc] showed the highest cytotoxicity with an IC 50 of 5.8 µM. The complexes showed higher activity than free ligand due to the lipophilicity of the chelate. The group 10 metal complexes could be the promising cancer therapeutic agents. The lowest binding energy of -8.16 kcal/mol among all the tested compounds was found for [PdL.dmso] using molecular docking of active site crystal structure of the tyrosine kinase domain of the EGFR (PDB: 1M17). [Display omitted] [ABSTRACT FROM AUTHOR]