| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1308617 | Inorganica Chimica Acta | 2012 | 8 Pages |
A series of oxovanadium(V) complexes, [VO2L1]2 (1), [VO2L2]2 (2), [VO2L3]2 (3), [VO2L4]2 (4), [VO(OCH3)L5] (5), and [VO(OCH3)(HOCH3)L6] (6) (HL1 = 2-ethoxy-6-{[2-(2-hydroxyethylamino)ethylimino]methyl}phenol, HL2 = 4-chloro-2-{[2-(2-hydroxyethylamino)ethylimino]methyl}phenol, HL3 = 2-methoxy-6-[(2-methylaminoethylimino)methyl]phenol, HL4 = 4-chloro-2-[(2-methylaminoethylimino)methyl]phenol, HL5 = N′-(2-hydroxy-3-ethoxybenzylidene)-3-hydroxy-2-naphthohydrazide, and HL6 = N′-(2-hydroxy-5-chlorobenzylidene)-3-hydroxy-2-naphthohydrazide), have been prepared and structurally characterized by physico-chemical methods and X-ray diffraction. The inhibition rates (%) with the concentration of 100 μM for the complexes on Helicobacter pylori urease are 18.96 ± 0.44 (1), 33.01 ± 1.80 (2), 35.83 ± 0.78 (3), 48.09 ± 1.23 (4), 45.91 ± 2.09 (5), and 90.72 ± 1.91 (6). The relationship between the structures and urease inhibitory activities indicates that the chloro-substituted complexes have stronger activity than the alkoxy-substituted complexes. It is notable that one of the chloro-substituted complexes has very strong urease inhibitory activity, with IC50 value of 17.35 ± 1.01 μM, which is much lower than that of the acetohydroxamic acid coassayed as a standard urease inhibitor. The kinetic studies reveal that the complex is a mixed-competitive inhibitor of urease. The molecular docking study of the complexes with the Helicobacter pylori urease was performed.
Graphical abstractA series of oxovanadium(V) complexes with Schiff bases have been prepared and structurally characterized. One chloro-substituted complex has effective urease inhibitory activity.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The use of oxovanadium complexes as urease inhibitor has seldom been reported. ► A series of oxovanadium complexes with Schiff bases has been prepared and characterized. ► The urease inhibitory activities of the complexes were studied. ► One complex shows strong urease inhibition. ► The kinetic study reveals that the complex is a mixed-competitive inhibitor of urease.
