1. Zinc(II) complexes of the second-generation quinolone antibacterial drug enrofloxacin: Structure and DNA or albumin interaction.
- Author
-
Tarushi A, Raptopoulou CP, Psycharis V, Terzis A, Psomas G, and Kessissoglou DP
- Subjects
- Albumins chemistry, Animals, Binding, Competitive drug effects, Cattle, Crystallography, X-Ray, DNA chemistry, Enrofloxacin, Ethidium, Humans, Models, Molecular, Molecular Conformation, Protein Binding, Serum Albumin, Bovine chemistry, Spectrometry, Fluorescence, Spectrometry, Mass, Electrospray Ionization, Spectrophotometry, Ultraviolet, Albumins drug effects, Anti-Bacterial Agents chemical synthesis, Anti-Bacterial Agents chemistry, DNA drug effects, Fluoroquinolones chemical synthesis, Fluoroquinolones chemistry, Intercalating Agents chemical synthesis, Intercalating Agents chemistry, Quinolones chemical synthesis, Quinolones chemistry, Zinc chemistry
- Abstract
Zinc mononuclear complexes with the second-generation quinolone antibacterial drug enrofloxacin in the absence or presence of a nitrogen donor heterocyclic ligand 1,10-phenanthroline or 2,2'-bipyridine have been synthesized and characterized. Enrofloxacin is on deprotonated mode acting as a bidentate ligand coordinated to zinc ion through the ketone and a carboxylato oxygen atoms. The crystal structure of bis(enrofloxacinato)(1,10-phenanthroline)zinc(II), 2, has been determined by X-ray crystallography. The biological activity of the complexes has been evaluated by examining their ability to bind to calf-thymus DNA (CT DNA) with UV and fluorescence spectroscopies. UV studies of the interaction of the complexes with DNA have shown that they can bind to CT DNA and the DNA binding constants have been calculated. Competitive studies with ethidium bromide (EB) have shown that the complexes exhibit the ability to displace the DNA-bound EB indicating that they bind to DNA in strong competition with EB for the intercalative binding site. The complexes exhibit good binding propensity to human and bovine serum albumin proteins having relatively high binding constant values., (Copyright 2010 Elsevier Ltd. All rights reserved.)
- Published
- 2010
- Full Text
- View/download PDF