Τίτλος:
Zinc(II) complexes of 3,5–dibromo–salicylaldehyde and α–diimines: Synthesis, characterization and in vitro and in silico biological profile
Περίληψη:
The synthesis of five neutral zinc(II) complexes of 3,5–dibromo–salicyladehyde (3,5–diBr–saloH) in the presence of nitrogen–donor co-ligands 2,2′–bipyridine (bipy), 1,10–phenanthroline (phen), 2,9–dimethyl–1,10–phenanthroline (neoc), or 2,2′–bipyridylamine (bipyam) was undertaken and complexes [Zn(3,5–diBr–salo)2(H2O)2] (1), [Zn(3,5–diBr–salo)2(bipy)] (2), [Zn(3,5–diBr–salo)2(phen)].3,5–diBr–saloΗ (3), [Zn(3,5–diBr–salo)2(neoc)] (4) and [Zn(3,5–diBr–salo)2(bipyam)] (5) were characterized by various techniques. The crystal structures of complexes 3 and 5 were determined by X–ray crystallography, revealing the co–existence of two different coordination modes of 3,5–diBr–salo− ligands. The new complexes show selective in vitro antibacterial activity against two Gram–positive and two Gram–negative bacterial strains. The complexes may scavenge 1,1–diphenyl–picrylhydrazyl and 2,2′–azinobis(3–ethylbenzothiazoline–6–sulfonic acid) radicals and reduce H2O2. The complexes may intercalate in–between the calf–thymus DNA–bases and have exhibited low–to–moderate 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 DNA–gyrase, 5–lipoxygenase, and 5–lipoxygenase 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.
Συγγραφείς:
Zianna, A.
Geromichalou, E.
Geromichalos, G.
Fiotaki, A.-M.
Hatzidimitriou, A.G.
Kalogiannis, S.
Psomas, G.
Λέξεις-κλειδιά:
3,5 dibromo salicyladehyde; antibiotic agent; antioxidant; arachidonate 5 lipoxygenase; ascorbic acid; bovine serum albumin; butylcresol; chlorobiocin; DNA; DNA topoisomerase (ATP hydrolysing); human serum albumin; hydrogen peroxide; ibuprofen; moxifloxacin; nordihydroguaiaretic acid; plasmid DNA; qpt 1; salicylaldehyde; trolox C; unclassified drug; warfarin; zinc complex; aldehyde; coordination compound; enzyme inhibitor; Escherichia coli protein; salicylaldehyde; zinc, antibacterial activity; antioxidant activity; Article; computer model; controlled study; crystal structure; deprotonation; DPPH radical scavenging assay; Escherichia coli; Fourier transform infrared spectroscopy; Gram negative bacterium; Gram positive bacterium; in vitro study; infrared spectroscopy; minimum inhibitory concentration; molecular docking; nonhuman; protein DNA interaction; proton nuclear magnetic resonance; Staphylococcus aureus; thymus; ultraviolet visible spectroscopy; X ray crystallography; Xanthomonas campestris; animal; bovine; chemistry; enzymology; human; metabolism; synthesis, Aldehydes; Animals; Cattle; Coordination Complexes; Enzyme Inhibitors; Escherichia coli; Escherichia coli Proteins; Humans; Staphylococcus aureus; Zinc
