8 research outputs found
Zinc(II) complexes of 3,5âdibromoâsalicylaldehyde and αâdiimines: Synthesis, characterization and in vitro and in silico biological profile
The synthesis of five neutral zinc(II) complexes of 3,5âdibromoâsalicyladehyde (3,5âdiBrâsaloH) in the presence of nitrogenâdonor co-ligands 2,2âČâbipyridine (bipy), 1,10âphenanthroline (phen), 2,9âdimethylâ1,10âphenanthroline (neoc), or 2,2âČâbipyridylamine (bipyam) was undertaken and complexes [Zn(3,5âdiBrâsalo)2(H2O)2] (1), [Zn(3,5âdiBrâsalo)2(bipy)] (2), [Zn(3,5âdiBrâsalo)2(phen)].3,5âdiBrâsaloÎ (3), [Zn(3,5âdiBrâsalo)2(neoc)] (4) and [Zn(3,5âdiBrâsalo)2(bipyam)] (5) were characterized by various techniques. The crystal structures of complexes 3 and 5 were determined by Xâray crystallography, revealing the coâexistence of two different coordination modes of 3,5âdiBrâsaloâ ligands. The new complexes show selective in vitro antibacterial activity against two Gramâpositive and two Gramânegative bacterial strains. The complexes may scavenge 1,1âdiphenylâpicrylhydrazyl and 2,2âČâazinobis(3âethylbenzothiazolineâ6âsulfonic acid) radicals and reduce H2O2. The complexes may intercalate inâbetween the calfâthymus DNAâbases and have exhibited lowâtoâmoderate ability to cleave supercoiled circular pBR322 plasmid DNA. The complexes may bind tightly and reversibly to bovine and human serum albumins. In order to explain the in vitro activity of the compounds, molecular docking studies were adopted on the crystal structure of calf-thymus DNA, human and bovine serum albumin, Escherichia coli and Staphylococcus aureus DNAâgyrase, 5âlipoxygenase, and 5âlipoxygenase activating protein. The employed in silico studies aimed to explore the ability of the compounds to bind to these target biomacromolecules, establishing a possible mechanism of action and were in accordance with the in vitro studies. © 2021 Elsevier Inc