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Acta Polymerica     Hybrid Journal   (Followers: 6)
Additives for Polymers     Full-text available via subscription   (Followers: 21)
Advances in Inorganic Chemistry     Full-text available via subscription   (Followers: 4)
Advances in Polymer Technology     Hybrid Journal   (Followers: 11)
Annual Reports Section A (Inorganic Chemistry)     Full-text available via subscription   (Followers: 2)
Bioinorganic Chemistry and Applications     Open Access   (Followers: 4)
Comments on Inorganic Chemistry: A Journal of Critical Discussion of the Current Literature     Hybrid Journal  
Current Methods in Inorganic Chemistry     Full-text available via subscription  
European Journal of Inorganic Chemistry     Hybrid Journal   (Followers: 6)
European Polymer Journal     Hybrid Journal   (Followers: 41)
Heterocyclic Communications     Full-text available via subscription   (Followers: 2)
High Performance Polymers     Hybrid Journal  
Indian Journal of Chemistry - Section A     Open Access   (Followers: 5)
Inorganic Chemistry     Full-text available via subscription   (Followers: 19)
Inorganic Chemistry Communications     Hybrid Journal   (Followers: 7)
Inorganic Chemistry Frontiers     Full-text available via subscription  
Inorganic Materials     Hybrid Journal   (Followers: 2)
Inorganic Materials: Applied Research     Hybrid Journal   (Followers: 1)
Inorganica Chimica Acta     Hybrid Journal   (Followers: 4)
Inorganics     Open Access  
International Journal of Inorganic Chemistry     Open Access   (Followers: 1)
JBIC Journal of Biological Inorganic Chemistry     Hybrid Journal   (Followers: 2)
Journal of Inorganic and Organometallic Polymers and Materials     Partially Free   (Followers: 6)
Journal of Inorganic Biochemistry     Hybrid Journal   (Followers: 2)
Journal of Inorganic Chemistry     Open Access  
Journal of Polymer Engineering     Full-text available via subscription   (Followers: 8)
Journal of Polymers and the Environment     Hybrid Journal   (Followers: 3)
Journal of Separation Science     Hybrid Journal   (Followers: 7)
Metallodrugs     Open Access  
Open Journal of Inorganic Chemistry     Open Access   (Followers: 1)
Plasmas and Polymers     Hybrid Journal  
Polymer Bulletin     Hybrid Journal   (Followers: 7)
Polymer Composites     Hybrid Journal   (Followers: 8)
Polyoxometalate Chemistry     Open Access  
Reviews in Inorganic Chemistry     Full-text available via subscription  
Russian Journal of Inorganic Chemistry     Hybrid Journal  
Studies in Inorganic Chemistry     Full-text available via subscription  
Synthesis and Reactivity in Inorganic, Metal-Organic, and Nano-Metal Chemistry     Hybrid Journal   (Followers: 3)
Topics in Inorganic and General Chemistry     Full-text available via subscription  
Zeitschrift für anorganische und allgemeine Chemie     Hybrid Journal   (Followers: 1)
Zeitschrift für Kristallographie - New Crystal Structures     Open Access  
Journal Cover Journal of Inorganic Biochemistry     [SJR: 0.807]   [H-I: 79]
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   Hybrid Journal Hybrid journal (It can contain Open Access articles)
   ISSN (Print) 0162-0134
   Published by Elsevier Homepage  [2582 journals]
  • The gallium(III)–salicylidene acylhydrazide complex shows
           synergistic anti-biofilm effect and inhibits toxin production by
           Pseudomonas aeruginosa
    • Abstract: Publication date: September 2014
      Source:Journal of Inorganic Biochemistry, Volume 138
      Author(s): Olena Rzhepishevska , Shoghik Hakobyan , Barbro Ekstrand-Hammarström , Yvonne Nygren , Torbjörn Karlsson , Anders Bucht , Mikael Elofsson , Jean-François Boily , Madeleine Ramstedt
      Bacterial biofilms cause a range of problems in many areas and especially in health care. Biofilms are difficult to eradicate with traditional antibiotics and consequently there is a need for alternative ways to prevent and/or remove bacterial biofilms. Furthermore, the emergence of antibiotic resistance in bacteria creates a challenge to find new types of antibiotics with a lower evolutionary pressure for resistance development. One route to develop such drugs is to target the so called virulence factors, i.e. bacterial systems used when bacteria infect a host cell. This study investigates synergy effects between Ga(III) ions, previously reported to suppress biofilm formation and growth in bacteria, and salicylidene acylhydrazides (hydrazones) that have been proposed as antivirulence drugs targeting the type three secretion system used by several Gram-negative pathogens, including Pseudomonas aerugionosa, during bacterial infection of host cells. A library of hydrazones was screened for: Fe(III) binding, enhanced anti-biofilm effect with Ga(III) on P. aeruginosa, and low cytotoxicity to mammalian cells. The metal coordination for the most promising ligand, 2-Oxo-2-[N-(2,4,6-trihydroxy-benzylidene)-hydrazino]-acetamide (ME0163) with Ga(III) was investigated using extended X-ray absorption fine structure spectroscopy as well as density functional theory. The results showed that Ga(III) chelates the hydrazone with 5- and 6-membered chelating rings, and that the Ga(III)–ME0163 complex enhanced the antibiofilm effect of Ga(III) while suppressing the type three secretion system in P. aeruginosa. The latter effect was not observed for the hydrazone alone and was similar for Ga(III)–citrate and Ga(III)–ME0163 complexes, indicating that the inhibition of virulence was caused by Ga(III).
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • Proton and gallium(III) binding properties of a biologically active
           salicylidene acylhydrazide
    • Abstract: Publication date: September 2014
      Source:Journal of Inorganic Biochemistry, Volume 138
      Author(s): Shoghik Hakobyan , Jean-François Boily , Madeleine Ramstedt
      Bacterial biofilm formation causes a range of problems in our society, especially in health care. Salicylidene acylhydrazides (hydrazones) are promising antivirulence drugs targeting secretion systems used during bacterial infection of host cells. When mixed with the gallium ion they become especially potent as bacterial and biofilm growth-suppressing agents, although the mechanisms through which this occurs are not fully understood. At the base of this uncertainty lies the nature of hydrazone–metal interactions. This study addresses this issue by resolving the equilibrium speciation of hydrazone–gallium aqueous solutions. The protonation constants of the target 2-oxo-2-[N-(2,4,6-trihydroxy-benzylidene)-hydrazino]-acetamide (ME0163) hydrazone species and of its 2,4,6-trihydroxybenzaldehyde and oxamic acid hydrazide building blocks were determined by UV–visible spectrophotometry to achieve this goal. These studies show that the hydrazone is an excessively strong complexing agent for gallium and that its antivirulence properties are predominantly ascribed to monomeric 1:1Ga–ME0163 complexes of various Ga hydrolysis and ME0163 protonation states. The chelation of Ga(III) to the hydrazone also increased the stability of the compounds against acid-induced hydrolysis, making this group of compounds very interesting for biological applications where the Fe-antagonist action of both Ga(III) and the hydrazone can be combined for enhanced biological effect.
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • Mechanism of reaction of chlorite with mammalian heme peroxidases
    • Abstract: Publication date: June 2014
      Source:Journal of Inorganic Biochemistry, Volume 135
      Author(s): Christa Jakopitsch , Katharina F. Pirker , Jörg Flemmig , Stefan Hofbauer , Denise Schlorke , Paul G. Furtmüller , Jürgen Arnhold , Christian Obinger
      This study demonstrates that heme peroxidases from different superfamilies react differently with chlorite. In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range. Chlorite acts as efficient one-electron donor for Compound I and Compound II of MPO and LPO and reacts with the corresponding ferric resting states in a biphasic manner. The first (rapid) phase is shown to correspond to the formation of a MPO-chlorite high-spin complex, whereas during the second (slower) phase degradation of the prosthetic group was observed. Cyanide, chloride and hydrogen peroxide can block or delay heme bleaching. In contrast to HRP, the MPO/chlorite system does not mediate chlorination of target molecules. Irreversible inactivation is shown to include heme degradation, iron release and decrease in thermal stability. Differences between mammalian peroxidases and HRP are discussed with respect to differences in active site architecture and heme modification.
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • Guanidine platinum(II) complexes: synthesis, in vitro antitumor activity,
           and DNA interactions
    • Abstract: Publication date: April 2014
      Source:Journal of Inorganic Biochemistry, Volume 133
      Author(s): Anton A. Legin , Michael A. Jakupec , Nadezhda A. Bokach , Marina R. Tyan , Vadim Yu. Kukushkin , Bernhard K. Keppler
      The novel guanidine compounds trans-[Pt(NH2Me)2{NH=C(NHMe)NR}2](Cl)2 (R=NEt2 [7], NC5H10 [8]) (trans-7,8) were synthesized by the nucleophilic addition of methylamine to dialkylcyanamide ligands of the push–pull nitrile complexes trans-[PtCl2(RCN)2] (R=NEt2, NC5H10). In vitro cytotoxicity tests conducted for the entire series of the guanidine complexes, i.e. trans-7,8, the neutral cis- or trans-[PtCl2{NH=C(NH2)R}2] (cis-1–3 and trans-1–3) and the cationic cis- or trans-[Pt(NH3)2{NH=C(NH2)R}2](Cl)2 (cis-4–6 and trans-4–6) (R=NMe2 [1,4], NEt2 [2,5], NC5H10 [3,6]) in two human cancer cell lines, CH1 (ovarian carcinoma) and SW480 (colon cancer), confirmed that the cytotoxicity of several trans-configured (trans-3,6) complexes is higher than that of cis-congeners (cis-3,6). Cellular platinum levels were analyzed by inductively coupled plasma mass spectrometry upon treatment of SW480 cells, revealing a dependence of cellular accumulation on the geometrical isomerism and the steric hindrance of the variable substituent R on the guanidine ligand. DNA interactions of selected guanidine complexes were studied in order to find hints for the possible reasons for their different activities. Changes induced to the electrophoretic mobility of a dsDNA plasmid confirmed the potency of the guanidine complexes (e.g. trans-1,3,5,6 and cis-1,3,4) to significantly alter DNA secondary structure, indicating DNA as a possible critical target of these compounds.
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • Real-time detection of DNA cleavage induced by
           [M(2,2′-bipyridine)2(NO3)](NO3) (M=Cu(II), Zn(II) and Cd(II))
           complexes using linear dichroism technique
    • Abstract: Publication date: October 2013
      Source:Journal of Inorganic Biochemistry, Volume 127
      Author(s): Hee-Jin Park , Ji Hye Kwon , Tae-Sub Cho , Jong Moon Kim , In Hong Hwang , Cheal Kim , Soojin Kim , Jinheung Kim , Seog K. Kim
      The catalytic effect of [M(2,2′-bipyridine)2(NO3)](NO3) (M(bpy)2, M=Cu(II), Zn(II) and Cd(II)) on the super-coiled and double stranded DNA (scDNA and dsDNA) was examined by electrophoresis and a real-time detection linear dichroism (LD) technique. Although the Cu(bpy)2 complex effectively cleaved both types of DNA, the other two complexes were inactive. This was explained by the electrochemical properties of the metal complexes. The Cu(bpy)2 complex exhibited a redox potential at −0.222V with a peak to peak separation of 0.201V, whereas the other two metal complexes did not undergo any redox reaction. Both electrophoresis and LD measurements revealed the superoxide radical, ·O2 −, to be responsible for DNA cleavage. A kinetic study using the LD technique showed that the cleavage of dsDNA consisted of two first order reactions. The fast reaction is believed to reflect the cleavage of one strand, whereas the slow reaction involves the cleavage of the complementary strand at or near the first cleaved site.
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • Biological activity of ruthenium and osmium arene complexes with modified
           paullones in human cancer cells
    • Abstract: Publication date: November 2012
      Source:Journal of Inorganic Biochemistry, Volume 116
      Author(s): Gerhard Mühlgassner , Caroline Bartel , Wolfgang F. Schmid , Michael A. Jakupec , Vladimir B. Arion , Bernhard K. Keppler
      In an attempt to combine the ability of indolobenzazepines (paullones) to inhibit cyclin-dependent kinases (Cdks) and that of platinum-group metal ions to interact with proteins and DNA, ruthenium(II) and osmium(II) arene complexes with paullones were prepared, expecting synergies and an increase of solubility of paullones. Complexes with the general formula [MIICl(η 6-p-cymene)L]Cl, where M=Ru (1, 3) or Os (2, 4), and L= L 1 (1, 2) or L 2 (3, 4), L 1 = N-(9-bromo-7,12-dihydroindolo[3,2-d][1]-benzazepin-6(5H)-yliden-N′-(2-hydroxybenzylidene)azine and L 2 = N-(9-bromo-7,12-dihydroindolo[3,2-d][1]benzazepin-6-yl)-N′-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl-methylene]azinium chloride (L 2 *HCl), were now investigated regarding cytotoxicity and accumulation in cancer cells, impact on the cell cycle, capacity of inhibiting DNA synthesis and inducing apoptosis as well as their ability to inhibit Cdk activity. The MTT (3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide) assay yielded IC50 values in the nanomolar to low micromolar range. In accordance with cytotoxicity data, the BrdU assay showed that 1 is the most and 4 the least effective of these compounds regarding inhibition of DNA synthesis. Effects on the cell cycle are minor, although concentration-dependent inhibition of Cdk2/cyclin E activity was observed in cell-free experiments. Induction of apoptosis is most pronounced for complex 1, accompanied by a low fraction of necrotic cells, as observed by annexin V–fluorescein isothiocyanate/propidium iodide staining and flow cytometric analysis.
      Graphical abstract image Highlights Ruthenium and osmium arene complexes with modified paullone ligands strongly inhibit cancer cell growth. Antiproliferative activity correlates with inhibition of DNA synthesis and induction of apoptosis, but seems to be independent of Cdk inhibition, given the moderate potency of inhibiting Cdk2/cyclin E and the lack of pronounced cell cycle effects. ► Ru and Os arene complexes with Paullone ligands strongly inhibit cancer cell growth. ► Cytotoxicity correlates with inhibition of DNA synthesis and induction of apoptosis. ► Cdk2/cyclin E inhibition and cell cycle effects insufficiently explain cytotoxicity.

      PubDate: 2015-01-09T18:42:26Z
  • Osmium(IV) complexes with 1H- and 2H-indazoles: Tautomer identity versus
           spectroscopic properties and antiproliferative activity
    • Abstract: Publication date: August 2012
      Source:Journal of Inorganic Biochemistry, Volume 113
      Author(s): Gabriel E. Büchel , Iryna N. Stepanenko , Michaela Hejl , Michael A. Jakupec , Bernhard K. Keppler , Petra Heffeter , Walter Berger , Vladimir B. Arion
      A one-pot synthesis of osmium(IV) complexes with two different tautomers of indazole, 1H-indazole and 2H-indazole, namely (H2ind)[OsIVCl5(2H-ind)] (1) and (H2ind)[OsIVCl5(1H-ind)] (2) is reported. Both compounds have been comprehensively characterized by NMR spectroscopy, ESI (electrospray ionization) mass spectrometry, electronic absorption spectroscopy, IR spectroscopy, cyclic voltammetry and tested for antiproliferative activity in vitro in three human cancer cell lines, CH1 (ovarian carcinoma), A549 (non-small cell lung cancer) and SW480 (colon carcinoma), as well as in vivo in a Hep3B SCID mouse xeno-transplantation model. 2H-Indazole tautomer stabilization in 1 has been confirmed by X-ray diffraction.
      Graphical abstract image Highlights A one-pot synthesis of (H2ind)[OsIVCl5(2H-ind)] and (H2ind)[OsIVCl5(1H-ind)] is reported. Both compounds have been characterized and tested for antiproliferative activity in vitro in three human cancer cell lines CH1, A549 and SW480 as well as in vivo in the Hep3B SCID mouse xeno-transplantation model. 2H-Indazole tautomer stabilization in (H2ind)[OsIVCl5(2H-ind)], which is very rare in the coordination chemistry of indazole, has been confirmed by X-ray diffraction. ► One-pot synthesis of osmium(IV) complexes with two different indazole tautomers. ► Spectroscopic behavior, solvatochromism. ► In vitro and in vivo cytotoxic activity of (H2ind)[OsCl5(1H-ind)] and (H2ind)[OsCl5(2H-ind)].

      PubDate: 2015-01-09T18:42:26Z
  • Influence of pH on the speciation of copper(II) in reactions with the
           green tea polyphenols, epigallocatechin gallate and gallic acid
    • Abstract: Publication date: July 2012
      Source:Journal of Inorganic Biochemistry, Volume 112
      Author(s): Katharina F. Pirker , Maria Camilla Baratto , Riccardo Basosi , Bernard A. Goodman
      Changes in speciation of copper(II) in reactions with epigallocatechin gallate (EGCG) and gallic acid (GA) as a function of pH have been investigated by multifrequency (X- and S-band) EPR spectroscopy in the fluid and frozen states. The EPR spectra show the formation of three distinct mononuclear species with each of the polyphenols, and these are interpreted in terms of one mono- and two bis-complexes. However, di- or polymeric complexes dominate the Cu(II) speciation in the pH range 4–8, and it is only at alkaline pH values that these mononuclear complexes make appreciable contributions to the metal speciation. Each mononuclear complex displays linewidth anisotropy in fluid solution as a consequence of incomplete averaging of the spin Hamiltonian parameters through molecular motion. Rotational correlation times for the individual complexes have been estimated by analysing the lineshape anisotropy of the fluid solution spectra using parameters determined by simulation of the rigid limit spectra. These show that the molecular masses increase with increasing pH, indicating either coordination of increasing numbers of polyphenol molecules as ligands to the copper or the increasing involvement of polyphenol dimers as ligands in the copper coordination sphere.
      Graphical abstract image Highlights Reactions of Cu2+ with GA and EGCG produce complexes at pH>8, but polymeric species at lower pH. ► Cu(II) speciation with two polyphenols (EGCG and GA) at different pH. ► EPR study at two frequencies (X- and S-band). ► Polymerisation dominates at slightly acidic and neutral pH. ► Complexation dominates above neutral pH.

      PubDate: 2015-01-09T18:42:26Z
  • Radical production by hydrogen peroxide/bicarbonate and copper uptake in
           mammalian cells: Modulation by Cu(II) complexes
    • Abstract: Publication date: February 2011
      Source:Journal of Inorganic Biochemistry, Volume 105, Issue 2
      Author(s): Larissa C. Carvalho do Lago , Andreza C. Matias , Cassiana S. Nomura , Giselle Cerchiaro
      The presence of the bicarbonate/carbon dioxide pair is known to accelerate the transition metal ion-catalysed oxidation of various biotargets. It has been shown that stable Cu(II) complexes formed with imine ligands that allow redox cycling between Cu(I) and Cu(II) display diverse apoptotic effects on cell cultures. It is also reported that Cu(II)–tetraglycine can form a stable Cu(III) complex. In the present study, radical generation from H2O2 and H2O2/HCO3 − in the presence of these two different classes of Cu(II) complexes was evaluated by monitoring the oxidation of dihydrorhodamine 123 and NADH and by the quantitative determination of thiobarbituric acid reactive substances (TBARs method). Cu(II)–imine complexes produced low levels of reactive species whereas Cu(II)–Gly-derived complexes, as well as the free Cu(II) ion, produced oxygen-derived radicals in significantly larger amounts. The effects of these two classes of complexes on mammalian tumour cell viability were equally distinct, in that Cu(II)–imine complexes caused apoptosis, entered in cell and remained almost unaffected in high levels whilst, at the same concentrations, Cu(II)–Gly peptide complexes and Cu(II) sulphate stimulated cell proliferation, with the cell managing copper efficiently. Taken together, these results highlight the different biological effects of Cu(II) complexes, some of which have been recently studied as anti-tumour drugs and radical system generators, and also update the effects of reactive oxygen species generation on cell cycle control.
      Graphical abstract image

      PubDate: 2015-01-09T18:42:26Z
  • The behaviour of myo-inositol hexakisphosphate in the presence of
           magnesium(II) and calcium(II): Protein-free soluble InsP6 is limited to
           49μM under cytosolic/nuclear conditions
    • Abstract: Publication date: November 2006
      Source:Journal of Inorganic Biochemistry, Volume 100, Issue 11
      Author(s): Nicolás Veiga , Julia Torres , Sixto Domínguez , Alfredo Mederos , Robin F. Irvine , Alvaro Díaz , Carlos Kremer
      Progress in the biology of myo-inositol hexakisphosphate (InsP 6) has been delayed by the lack of a quantitative description of its multiple interactions with divalent cations. Our recent initial description of these [J. Torres, S. Dominguez, M.F. Cerda, G. Obal, A. Mederos, R.F. Irvine, A. Diaz, C. Kremer, J. Inorg. Biochem. 99 (2005) 828–840] predicted that under cytosolic/nuclear conditions, protein-free soluble InsP 6 occurs as Mg5(H2L), a neutral complex that exists thanks to a significant, but undefined, window of solubility displayed by solid Mg5(H2L)·22H2O (L is fully deprotonated InsP 6). Here we complete the description of the InsP 6–Mg2+–Ca2+ system, defining the solubilities of the Mg2+ and Ca2+ (Ca5(H2L)·16H2O) solids in terms of K s0 =[M2+]5[H2L10−], with pK s0 =32.93 for M=Mg and pK s0 =39.3 for M=Ca. The concentration of soluble Mg5(H2L) at 37°C and I =0.15M NaClO4 is limited to 49μM, yet InsP 6 in mammalian cells may reach 100μM. Any cytosolic/nuclear InsP 6 in excess of 49μM must be protein- or membrane-bound, or as solid Mg5(H2L)·22H2O, and any extracellular InsP 6 (e.g. in plasma) is surely protein-bound.

      PubDate: 2015-01-09T18:42:26Z
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