Supramolecular Heteroleptic Copper(II) Carboxylates: Synthesis, Spectral Characterization, Crystal Structures, and Enzyme Inhibition Assay.

Two new complexes of substituted phenyl acetic acids with CuSO 4 . 5H 2 O and 2,2'-bipyridine (Bipy) with formula [CuL(Bipy) 2 ]L . nH 2 O, where L = 2-ClC 6 H 4 CH 2 COO- (I), 2-CH 3 -3-NO 2 C 6 H 3 CH 2 COO- (II) and n = 3 (I); 4 (II), have been synthesized. These complexes have been characterized by elemental analysis, FT-IR and X-ray crystal diffraction (CIF file CCDC nos. 1487707 (I), 1487708 (II)). Both complexes are mononuclear and crystallize in the triclinic space group P¯1. In both complexes two molecules of Bipy bind equatorially with metal atom and one molecule of substituted phenyl acetic acid binds at axial position giving rise to a distorted five coordinated geometry around copper atom, while the second oxygen atom of carboxylate ligand appears to occupy the sixth position resulting in highly distorted six coordination environments around metal center in both complexes. However, another molecule of substituted phenyl acetic acid along with water molecules lies as co-crystal within the crystal lattice. Two bipyridine molecules in both complexes are lying in different planes and are oriented at dihedral angle of 63.89(8) ° and 74.99(11) ° in complexes I and II, respectively. Extensive hydrogen bonding because of water molecules present in crystal lattice plays a vital role in the formation of the 3D structure. Additionally, other weak interactions such as π-π interactions markedly influence the supramolecular structure. An investigation of DNA binding ability of both complexes using UV-visible spectroscopy and anti-diabetic capacity is also presented. Results revealed that synthesized complexes bind with SSDNA through intercalation as well as groove binding mode with Kb values of 2.45 × 10 4 and 7.72 × 10 3 M -1 for complex I and II, respectively. Complex II strongly inhibits in-vitro α-glucosidase with IC 50 value of 30.4 μM, while complex I moderately inhibits in-vitro α-amylase with IC50 value of 69.9 μM. Acarbose was employed as standard in both assays. [ABSTRACT FROM AUTHOR]

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