SYNTHESIS, STRUCTURAL CHARACTERIZATION AND ANTIMICROBIAL STUDIES OF NOVEL SCHIFF BASE COPPER(II) COMPLEXES

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Abstract

Five novel copper(II) complexes have been synthesized using Schiff base ligands, synthesized by the condensation reaction of anthranilic acid and Knoevenagel β-ketoanilide condensates (obtained by the condensation of acetoacetanilide and substituted benzaldehydes). The ligands and copper(II) complexes have been characterized on the basis of Microanalytical, Mass, UV-Vis., IR, 'H NMR, ESR, XRD and CV spectral studies, as well as magnetic susceptibility and conductivity data. On the basis of spectral studies, a square-planar geometry has been proposed for the copper(II) complexes. From the XRD data, the CuL-1 complex has the crystallite size of 50 nm respectively. The in vitro antimicrobial activity of the compounds is tested against the bacteria Escherichia coli, Salmonella typhi, Staphylococcus aureus, Klebsiella pneumoniae and Pseudonomas aeruginosa and fungi Aspergillus niger, Rhizopus stolonifer, Aspergillus flavus, Rhizoctonia bataicola and Candida albicans by well diffusion method. The complexes show stronger antimicrobial activity than the free ligands. They represent a novel class of metal-based antimicrobial agents which provide opportunities for a large number of synthetic variations for modulation of the activities.

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Identification of small molecular weight inhibitors of Src homology 2 domain-containing tyrosine phosphatase 2 (SHP-2) via in silico database screening combined with experimental assay.

Olgun Guvench, Cheng-Kui Qu, Xiao-Mei Yu … (2008)

Virtual screening methods combined with experimental assays were used to identify low molecular weight inhibitors for Src homology 2 domain-containing phosphatase 2 (SHP-2) that is mutated and hyperactivated in Noonan syndrome and a significant portion of childhood leukemias. Virtual screening included multiple conformations of the protein, score normalization procedures, and chemical similarity considerations. As the catalytic core of SHP-2 shares extremely high homology to those of the related SHP-1 phosphatase and other tyrosine phosphatases, in order to identify selective inhibitors, we chose to target an adjacent protein surface pocket that is predicted to be important for binding to phosphopeptides and that has structural features unique to SHP-2. From a database of 1.3 million compounds, 9 out of 165 computationally selected compounds were shown to inhibit SHP-2 activity with IC(50) values of approximately 100 microM. Two of the active compounds were further verified for their ability to inhibit SHP-2-mediated cellular functions. Fluorescence titration experiments confirmed their direct binding to SHP-2. Because of their simple chemical structures, these small organic compounds have the potential to act as lead compounds for the development of novel anti-SHP-2 drugs.