Structural, Antioxidant, and Protein/DNA-Binding Properties of Sulfate-Coordinated Ni(II) Complex with Pyridoxal-Semicarbazone (PLSC) Ligand

• Published in: Inorganics 2024-11, Vol.12 (11), p.280
• Main Authors: Jevtovic, Violeta, Golubović, Luka, Alshammari, Odeh A. O., Alhar, Munirah Sulaiman, Alanazi, Tahani Y. A., Radulović, Aleksandra, Nakarada, Đura, Dimitrić Marković, Jasmina, Rakić, Aleksandra, Dimić, Dušan
• Format: Article
• Language: English
• Subjects: Antioxidants; Atomic properties; Binding; Biological activity; Cancer; Chemical bonds; Coordination compounds; Crystal structure; Crystallography; DFT; EPR; Ethidium bromide; Free radicals; Geometry; HSA; Human serum albumin; Hydrogen bonds; Ligands; Metal ions; Molecular docking; Ni(II) complexes; Nickel; Nitrates; Nitrogen; Potassium iodide; Potassium iodides; Prostate; Pseudopotentials; pyridoxal-semicarbazone; Quantum theory; Quenching; Serum albumin; Spectroscopic analysis; Spectrum analysis; Stabilization; Surface analysis (chemical); Titration; Transition metal compounds; Vibration
• ISSN: 2304-6740; 2304-6740
• DOI: 10.3390/inorganics12110280

The pyridoxal-semicarbazone (PLSC) ligand and its transition metal complexes have shown significant biological activity. In this contribution, a novel nickel(II)-PLSC complex, [Ni(PLSC)(SO4)(H2O)2], was obtained, and its structure was determined by X-ray crystallographic analysis, FTIR, and UV-VIS spectroscopy. The sulfate ion is directly coordinated to the central metal ion. The intermolecular stabilization interactions were examined using Hirshfeld surface analysis. The crystal structure was optimized by a B3LYP functional using two pseudopotentials for nickel(II) (LanL2DZ and def2-TZVP) together with a 6-311++G(d,p) basis set for non-metallic atoms. The experimental and theoretical bond lengths and angles were compared, and the appropriate level of theory was determined. The stabilization interactions within the coordination sphere were investigated by the Quantum Theory of Atoms in Molecules (QTAIM). The antioxidant activity towards hydroxyl and ascorbyl radicals was measured by EPR spectroscopy. The interactions between Human Serum Albumin (HSA) and the complex were examined by spectrofluorimetric titration and a molecular docking study. The mechanism of binding to DNA was analyzed by complex fluorescence quenching, potassium iodide quenching, and ethidium bromide displacement studies in conjunction with molecular docking simulations.