Synthesis, inhibitory activity and molecular docking studies of two Cu(II) complexes against Helicobacter pylori urease

Figures & data

Table 1.  Hydrogen bonds arrangement in 1 and 2•3H₂O (Å, °).

D–H A	d(D–H)	d(H…A)	d(D…A)	<(DHA)
1
N1−H1B…O2^i	0.90	2.06	2.928(7)	162.3
N2−H2A…O4^ii	0.90	2.05	2.927(6)	165.6
N3−H3B…O7^iii	0.90	2.09	2.964(7)	164.7
N4−H4A…O6^iv	0.90	2.05	2.912(7)	158.8
Symmetry codes: (i)−x, 1− y, 1− z; (ii) 1− x, 1− y, 1− z; (iii) 1− x, 2− y,−z; (iv)−x, 2− y,−z
2•3H2O
O5−H5D…O6^i	0.835(10)	2.032(11)	2.863(3)	174(3)
O5−H5C…O7^ii	0.840(10)	1.919(11)	2.754(3)	173(3)
O6−H6D…O4	0.838(10)	1.990(16)	2.797(3)	161(3)
O6−H6E…N2^iii	0.840(10)	2.205(19)	2.976(3)	153(3)
O7−H7C…O6	0.844(10)	2.089(11)	2.930(4)	175(4)
O7−H7D…O8^iv	0.842(10)	1.928(14)	2.757(4)	168(4)
O8−H8C…O2	0.837(10)	1.950(13)	2.780(4)	171(4)
O8−H8D…N4^v	0.834(10)	2.31(2)	3.043(4)	147(3)
Symmetry codes: (i) 2 − x, 1 − y, 1 − z; (ii) x, y, 1 + z; (iii) x,−1 + y, z; (iv) 1− x, 1− y, 1− z; (v) x, 1 + y, z

Figure 1.  The structure of complex 1. (a) An ORTEP diagram showing the structure of 1 with selected atom-labelling and thermal ellipsoids plotted at 30% probability. (b) One-dimensional (1D) structure of 1 formed by intermolecular N−H O hydrogen bonds.

Table 2.  Inhibition of H. pylori urease by 1, 2, ligands and Cu(II) ion.

Tested materials	IC50 (µM)
Benzylamine	>100
4-Methylbenzoic acid	>100
5-Methylpyrazine-2-carboxylic acid	>100
Cu^2+	8.54 ± 0.12
1	3.23 ± 0.14
2	1.05 ± 0.21
Acetohydroxamic acid	42.47 ± 0.19

Figure 2.  Complex 2 is bound into H. pylori urease (entry 1E9Z in the Protein Data Bank). The dotted line shows the hydrogen bond.