The new Azo ligand and its metal complexes have been prepared and characterized The reaction of 4-nitroaniline and 2-hydroxy-1-naphthaldehyde in a 1: 1 mole ratio resulted in the synthesis of ((E)-2-hydroxy-3-((4-nitrophenyl) diazenyl)-1-naphthaldehyde)(HL). The separation of monomeric complexes was accomplished by reacting ((E)-2-hydroxy-3-((4-nitrophenyl) diazenyl)-1-naphthaldehyde)(HL) with Cr, Mn II, Co II, Ni II, and Cu II metal ions in a mole ratio of 2: 1 (L: M). Elemental microanalysis, magnetic susceptibility, conductance, FT-IR, electronic spectra, and 1 HNMR, 13 C-NMR, and mass spectra were among the analytical and spectroscopic techniques used to describe the products. Based on the data collected during the characterization process, six coordinates were determined. The ligand and its complexes were tested against certain bacteria and fungi. The findings acquired suggested that the metal complexes are more active against a variety of organisms have been studied as compared to the free ligand.
The effect of the aqueous extract of fenugreek seeds (Trigonella Foenum Graecum L.), Rhodium complex (?) with formula [RhL2CLH2O].1 1/2 ETOH and palladium (?) [pdl2].2ETOH,where L=2-hydroxy phenyl piperonalidine was studied on two cancer cell lines. The first cell line was intestine cancer of female albino mice (L20B), the second one was Rhabdomysarcomas (RD)cell line in human. The activity of the new complexes and the aqueous extract was compared to the well-known anticancer drug (cis-platin) by utilizing the in vitro system. The cell lines were treated with four concentrations of cis-platin 31.25,62.5,125 and 250 ?g/ml for 72 hour exposure time. The same concentrations were used with extract and the new complexes. This study showed that t
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A simple, economical and selective method employing ion pair dispersive liquid−liquid microextraction (DLLME) coupled with spectrophotometric determination of carbamazepine (CBZ) in pharmaceutical preparations and biological samples was developed. The method is based on reduction of Mo(VI) to Mo(V) using a combination of ammonium thiocyanate and ascorbic acid in acidic medium to form a red binary Mo(V) thiocyanate complex. After addition of CBZ to the complex, extraction of the formed CBZ−Mo(V)−(SCN)6 was performed using a mixture of methylene chloride and methanol. Then, the measurement of target complex was performed at the wavelength of 470 nm. The important extraction parameters affecting the efficiency of DLLME were studied and o
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Platinum (Pt) supported on sulfated zirconia (SZ) and HY-zeolite as a solid acid catalyst was synthesized successfully for isomerization reaction using precipitation and impregnation method. The physicochemical properties of the catalyst were characterized using various techniques including X-ray diffraction (XRD), Fourier transformation infra-red spectroscopy (FTIR), BET Surface area and pore volume, and Field Emission Scanning Electron Microscopy (FESEM). The prepared composite catalyst Pt/SZ-HY consisted of high Bronsted acidic sites and Lewis acidic sites. The addition of multi-walled carbon nanotubes (MWCNTs) to SZ increased the surface area and pore volume, resulting in smaller crystal sizes and a narrower particle size dist
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Cholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and BC
... Show MoreCholinesterases are among the most efficient enzymes known. They are divided into two groups: acetylcholinesterase (AChE) involved in the hydrolysis of the neurotransimitter acetylcholine, and butyrylcholinesterase (BChE) of unknown function. Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge. Human BChE has attracted attention because it can hydrolyze toxic esters and nerve agents. Here we analyze the complexes of cholinesterase with soman by describing the 3D geometry of the complex, the active site, the changes happened through the inhibition and provide a description for the mechanism of inhibition. Soman undergoes degradation in the active site of the AChE and B
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Twelve N-(6-sustirured benzothanol-2-y1) succinamic acids and 3-(6-substitted benzonathol-2-y1)-carbamoyl propionyl chloride were synthesized in good yields from reaction of benzonathol2-yl)