Novel Aminoketooxime Ligand and Its Cu(II) and Mn(II) Complexes: Synthesis, Characterization and Molecular Docking Studies

Abstract

A novel ligand, N, N 2-(4-methyl-1,2-phenylene)bis(2-(biphenyl-4-yl)-N 1-hydroxy-2-oxoacetimidamide) (H2L) with its Cu(II) and Mn(II) complexes were synthesized in this study. All compounds synthesized were also characterized by 1 Hand 13 C-NMR, the Fourier transform infrared, elemental analysis, inductively coupled plasma optical emission spectrometry, molar conductivity, magnetic susceptibility measurements and thermogravimetric analysis. Vascular endothelial growth factor-2 (VEGFR-2) and cyclooxygenase-2 (COX-2) inhibition is often used as a parameter for being a potent anticancer agent in docking studies. For this purpose, synthesized and characterized ligand was investigated by molecular docking study to test its inhibitory effect against angiogenic factors VEGFR-2 and COX-2.

Synthesis, Structural Characterization, X‐ray, Hirshfeld Surfaces, DFT calculations, In Silico ADME Approach and a Molecular Docking Study of a New Nickel(II) Complex

“…Figures S18‐S20 show the images of the interaction conformations of ligands L 1 and L 2 and CHD. The free energy of interaction of Complex 2 with the L. paracasei , S. mutans and S. mitis structures was lower than the free energy of CHD, suggesting that the complex is more stable, a fact observed for other metal complexes reported in the literature [9,32,33] . The free binding energy between Complex 2 and the bacteria was found to be −10.09 kcal/mol for L. paracasei while the greatest energy value was found for the S. mitis protein structure (−6.29 kcal/mol).…”

“…structures was lower than the free energy of CHD, suggesting that the complex is more stable, a fact observed for other metal complexes reported in the literature. [9,32,33] The free binding energy between Complex 2 and the bacteria was found to be À 10.09 kcal/mol for L. paracasei while the greatest energy value was found for the S. mitis protein structure (À 6.29 kcal/ mol). The docked pose between Complex 2 and L. paracasei (Figure 9D) shows a considerably strong H bond Å in length) involving the NÀ H group from the thiosemicarbazone ligand and an oxygen atom of amino acid Asn 145.…”

Fragmentation Study, Dual Anti-Bactericidal and Anti-Viral Effects and Molecular Docking of Cobalt(III) Complexes

“…On the other hand, the best free binding energy between CHD and bacteria was found for E. faecalis (−11.24 kcal/mol), followed by S. sanguinis (−9.49 kcal/mol), and the highest value was found for S. mitis (−3.03 kcal/mol). Energy derived from the cobalt complex interaction with the L. paracasei structure was lower compared to the energy derived from CHD interaction with the same bacteria structure, suggesting that the complex couple is more stable, a fact observed for other metal complexes in the literature [41,42]. This observation is also in accordance with the antibacterial assay results which show a higher biological activity for [Co(atc-Ph) 2 ] + (MIC/MBC = 0.39/0.39 µg/mL) than for CHD (MIC/MBC = 0.92/0.92 µg/mL).…”

In silico studies of isatinyl-2-aminobenzoylhydrazone transition metal complexes against cyclin-dependent kinase 6 (CDK6)

“…The transition metals Co (II), Ni (II), Cu (II) and Zn (II) coordinates ISABH in a 3D conformation and enables them to optimally match on 3NUP. This ability mainly relies on the electron affinity which relates to metalligand polarization [25]. Cross-docking of ISABH, Co-ISABH, Cu-ISABH, Ni-ISABH, and Zn-ISABH was perfomed against CDK-6 protein (PDB ID: 3NUP).…”