Characterization and Cytotoxic Assessment of Bis(2-hydroxy-3-carboxyphenyl)methane and Its Nickel(II) Complex

Author:

Ahmed Ayman H.1ORCID,Althobaiti Ibrahim O.2,Alenezy Ebtsam K.1,Asiri Yazeed M.3,Ghalab Sobhy4ORCID,Hussein Omar A.5

Affiliation:

1. Department of Chemistry, College of Science, Jouf University, Sakaka 72341, Saudi Arabia

2. Department of Chemistry, Faculty of Science, Islamic University of Madinah, Madinah 42351, Saudi Arabia

3. Department of Chemistry, College of Science, Taif University, P.O. Box 11099, Taif 21944, Saudi Arabia

4. Department of Physics, College of Science, Jouf University, Sakaka 72341, Saudi Arabia

5. Faculty of Medicine, Benha University, Benha 13518, Egypt

Abstract

A condensation reaction of salicylic acid with formaldehyde in the presence of sulfuric acid led to the synthesization of the bis(2-hydroxy-3-carboxyphenyl)methane (BHCM) ligand, which was subsequently allowed to bind with nickel (II) ions. In light of the information obtained from the elemental analyses (C, H, and M), spectral (IR, MS, 1H-NMR, and UV–Vis) and thermal and magnetic measurements, the most likely structures of the ligand and complex have been identified. It has been suggested that the BHCM coordinates in a tetradentate manner with two Ni(II) ions to produce an octahedral binuclear complex. The SEM and TEM morphology of the compounds showed spherical shapes. An X-ray diffraction analysis indicated a considerable difference in the diffraction patterns between BHCM (crystalline) and Ni–BHCM (amorphous), and the Scherrer equation was used to calculate the crystallite size. Some optical characteristics were estimated from UV–Vis spectra. The ligand and its nickel(II) complex underlie the range of semiconductors. It was verified that for human lung (A-549) cancer, the BHCM compound displayed a significant barrier to the proliferation test in noncancerous cells (human lung fibroblasts, WI-38), which was also undertaken. To demonstrate the binding affinities of the chosen compounds (BHCM and Ni–BHCM) in the receptor protein’s active site [PDB ID: 5CAO], a molecular docking (MD) study was carried out.

Funder

Deanship of Graduate Studies and Scientific Research at Jouf University

Publisher

MDPI AG

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