Synthesis, Characterization and Biological Profile of Cationic Cobalt Complexes with First-Generation Quinolones
The interaction of cobalt(II) with first-generation quinolones oxolinic acid (Hoxo), flumequine (Hflmq), pipemidic acid (Hppa) and cinoxacin (Hcx) in the presence of the <i>N</i>,<i>N′</i>-donor heterocyclic ligands 2,2′-bipyridine (bipy) or 1,10-phenanthroline (phen) afforde...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-06-01
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| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/30/12/2646 |
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| Summary: | The interaction of cobalt(II) with first-generation quinolones oxolinic acid (Hoxo), flumequine (Hflmq), pipemidic acid (Hppa) and cinoxacin (Hcx) in the presence of the <i>N</i>,<i>N′</i>-donor heterocyclic ligands 2,2′-bipyridine (bipy) or 1,10-phenanthroline (phen) afforded a series of novel cobalt complexes, namely [Co(bipy)<sub>2</sub>(oxo)](PF<sub>6</sub>)<sub>2</sub>·H<sub>2</sub>O (<b>1</b>), [Co(phen)<sub>2</sub>(oxo)](PF<sub>6</sub>)<sub>2</sub>·0.5CH<sub>3</sub>OH·0.5H<sub>2</sub>O (<b>2</b>), [Co(bipy)<sub>2</sub>(flmq)](PF<sub>6</sub>)<sub>2</sub>·0.5CH<sub>3</sub>OH·0.5H<sub>2</sub>O (<b>3</b>), [Co(bipy)<sub>2</sub>(ppa)](PF<sub>6</sub>)<sub>2</sub>·CH<sub>3</sub>OH·0.5H<sub>2</sub>O (<b>4</b>), [Co(phen)<sub>2</sub>(cx)](PF<sub>6</sub>)<sub>2</sub>·CH<sub>3</sub>OH·0.5H<sub>2</sub>O (<b>5</b>), and [Co(phen)<sub>2</sub>(flmq)](PF<sub>6</sub>)·0.5CH<sub>3</sub>OH·H<sub>2</sub>O (<b>6</b>). The characterization of the complexes involved physicochemical techniques, various spectroscopies and single-crystal X-ray crystallography. The affinity of complexes to calf-thymus (CT) DNA was monitored with various techniques, suggesting intercalation in-between the DNA-nucleobases as the most probable interaction mode, which may be combined with electrostatic interactions as a result of the cationic nature of the complexes. The affinity of the complexes for bovine and human serum albumin proteins was monitored, and the determined corresponding albumin-binding constants revealed a tight and reversible interaction. |
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| ISSN: | 1420-3049 |