Synthesis, X-Ray Structure, Hirshfeld Surface Analysis, DFT Calculations, and Molecular Docking Studies of Nickel(II) Complex with Thiosemicarbazone Derivative
| Autor: | Muhamad Fairus Noor Hassim, Uwaisulqarni M. Osman, Fazira Ilyana Abdul Razak, Suhana Arshad, Ainizatul Husna Anizaim, Sharmili Silvarajoo |
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| Rok vydání: | 2021 |
| Předmět: |
Article Subject
Chemistry Hydrogen bond Organic Chemistry Intermolecular force chemistry.chemical_element Biochemistry Inorganic Chemistry Metal Bond length chemistry.chemical_compound Nickel Crystallography visual_art Electrophile visual_art.visual_art_medium Density functional theory TP248.13-248.65 Derivative (chemistry) Biotechnology QD146-197 Research Article |
| Zdroj: | Bioinorganic Chemistry and Applications Bioinorganic Chemistry and Applications, Vol 2021 (2021) |
| ISSN: | 1687-479X 1565-3633 |
| DOI: | 10.1155/2021/5536902 |
| Popis: | This article presents both experimental and computational study of a new Ni(II) complex, namely, bis{2-(2-trifluoromethylbenzylidene)hydrazine-1-carbothioamido-κ2N2, S}nickel(II) (abbreviate as NiL2). The complex was synthesized and well characterized using various spectroscopic methods. The single X-ray crystallographic study revealed a distorted square planar geometry around Ni(II) metal ion centre in which the angles deviated from ideal 90° with a maximum value of 6.57° occupied by nitrogen and sulphur donor atoms. The theoretical bond lengths and angles for the NiL2 complex were obtained by using the B3LYP level of density function theory (DFT) with LANL2DZ/6-311G (d, p) basis sets. These results showed very good agreement with the experimental X-ray values. The electrophilicity index (ω = 50.233 eV) shows that the NiL2 complex is a very strong electrophile. In addition, strong F⋯H/H⋯F interactions with 28.5% of the total Hirshfeld surface analyses in NiL2 were obtained indicating that the complex could bind with protein effectively. Furthermore, the new NiL2 complex was docked with plasma retinol-binding protein 4 (RBP4) (PDB id: 5NU7), which implied that the NiL2 complex bound to Tyrosine 133 and Aspartate 102 amino acids via N-H intermolecular hydrogen bonds. |
| Databáze: | OpenAIRE |
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