Copper(II) complexes with meclofenamate ligands: Structure, interaction with DNA and albumins, antioxidant and anticholinergic activity

The interaction of copper(II) with the non-steroidal anti-inflammatory drug sodium meclofenamate (Na-mclf) in the presence or absence of the nitrogen-donor co-ligands pyridine (py) or 2,2′-bipyridylamine (bipyam), yielded the novel Cu(II) complexes [Cu2(mclf-O,O′)4(MeOH)2]·2MeOH (1·2MeOH), [Cu(mclf-O)2(py)3]·H2O·0.5MeOH (2·H2O·0.5MeOH) and [Cu(mclf-O,O′)2(bipyam)] (3). The characterization of the complexes was achieved by various techniques, including single-crystal X-ray crystallography. In order to study the binding mode and strength of the complexes to calf-thymus (CT) DNA, various techniques were employed which suggested intercalation between the DNA-bases as the most possible interaction mode. Competitive studies with ethidium bromide (EB) revealed the ability of the complexes to displace the EB from the EB-DNA adduct, verifying the intercalative binding mode. The affinity of the complexes to bovine and human serum albumin proteins (SAs) was investigated by fluorescence emission spectroscopy and the corresponding binding constants bear relatively high values, showing that the complexes bind tightly and possibly reversibly to SAs. The antioxidant activity of the complexes against 1,1-diphenyl-picrylhydrazyl (DPPH), 2,2′-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radicals and the ability to reduce H2O2 proved to be of significant magnitude. The in vitro inhibitory activity against the enzymes acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) was evaluated, in order to assess the anticholinergic ability of the complexes, which appeared promising. [Display omitted] •Three copper(II) complexes with meclofenamato ligands were characterized.•The complexes show noteworthy radical scavenging activity.•The complexes may bind tightly and reversibly to serum albumins.•Intercalation is the most possible binding mode of the complexes to calf-thymus DNA.•Complexes exhibit remarkable inhibitory activity against cholinesterase enzymes.