Repozytorium

New copper(I) complexes bearing lomefloxacin motif : spectroscopic properties, in vitro cytotoxicity and interactions with DNA and human serum albumin.

Autorzy

Urszula K. Komarnicka

Radosław Starosta

Agnieszka Kyzioł

Michał Płotek

Małgorzata Puchalska

Małgorzata Jeżowska-Bojczuk

Rok wydania

2016

Czasopismo

Journal of Inorganic Biochemistry

Numer woluminu

165

Strony

25-35

DOI

10.1016/j.jinorgbio.2016.09.015

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

In this paper we present lomefloxacin's (HLm, 2nd generation fluoroquinolone antibiotic agent) organic and in- organic derivatives: aminomethyl(diphenyl)phosphine (PLm), its oxide as well as new copper(I) iodide or copper(I) thiocyanate complexes with PLm and 2,9-dimethyl-1,10-phenanthroline (dmp) or 2,2′-biquinoline (bq) as the auxiliary ligands. The synthesized compounds were fully characterised by NMR, UV-Vis and lumines- cence spectroscopies. Selected structures were analysed by theoretical DFT (density functional theory) methods. High stability of the complexes in aqueous solutions in the presence of atmosferic oxygen was proven. Cytotoxic activity of all compounds was tested towards three cancer cell lines (CT26 - mouse colon carcinoma, A549 - human lung adenocarcinoma, and MCF7 - human breast adenocarcinoma). All complexes are characterised by cytotoxic activity higher than the activity of the parent drug and its organic derivatives as well as cisplatin. Stud- ied derivatives as well as parent drug do not intercalate to DNA, except Cu(I) complexes with bq ligand. All stud- ied complexes caused single-stranded cleavage of the sugarphosphate backbone of plasmid DNA. The addition ofH2O2caused distinct changes inthe plasmidstructure and led to single-and/or double-strain plasmid cleavage. Studied compounds interact with human serum albumin without affecting its secondary structure.

Słowa kluczowe

Copper(I) complexes, cytotoxicity, Lomefloxacin, luminescence, Phosphines

Adres publiczny

http://dx.doi.org/10.1016/j.jinorgbio.2016.09.015

Strona internetowa wydawcy

http://www.elsevier.com

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