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

The ligand H2Lwith 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 CH3COO -. FTIR, UV-Vis, and 1 H and 13 C 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 IC50 of 15.6 mu M and a selectivity index (SI) of 2.8 against Hela.The complexes Na[NiL.OAc] and [PtL.dmso]exhibited significant activity against Hela with IC50 of 105.7 mu M and IC50 of 166 mu M respectively, whereas the ligand showed very poor activity. The complexes [PdL.dmso], [PtL.dmso] and ligand, H2L exhibited moderate activity against normal Eahy926 with IC50 values of 43.3 mu M, 45 mu M, and 185 mu M, respectively whereas, the Na[NiL.OAc]showed the highest cytotoxicity with an IC50 of 5.8 mu M. 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). (c) 2023 Elsevier B.V. All rights reserved.