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  Subjects -> CHEMISTRY (Total: 846 journals)
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INORGANIC CHEMISTRY (41 journals)

Showing 1 - 41 of 41 Journals sorted alphabetically
Acta Polymerica     Hybrid Journal   (Followers: 9)
Additives for Polymers     Full-text available via subscription   (Followers: 20)
Advances in Inorganic Chemistry     Full-text available via subscription   (Followers: 9)
Advances in Polymer Technology     Hybrid Journal   (Followers: 13)
Annual Reports Section A (Inorganic Chemistry)     Full-text available via subscription   (Followers: 3)
Bioinorganic Chemistry and Applications     Open Access   (Followers: 9)
Comments on Inorganic Chemistry: A Journal of Critical Discussion of the Current Literature     Hybrid Journal   (Followers: 2)
Current Methods in Inorganic Chemistry     Full-text available via subscription   (Followers: 2)
European Journal of Inorganic Chemistry     Hybrid Journal   (Followers: 12)
European Polymer Journal     Hybrid Journal   (Followers: 41)
Heterocyclic Communications     Hybrid Journal  
High Performance Polymers     Hybrid Journal   (Followers: 1)
Indian Journal of Chemistry - Section A     Open Access   (Followers: 7)
Inorganic Chemistry     Full-text available via subscription   (Followers: 24)
Inorganic Chemistry Communications     Hybrid Journal   (Followers: 11)
Inorganic Chemistry Frontiers     Full-text available via subscription   (Followers: 3)
Inorganic Materials     Hybrid Journal   (Followers: 4)
Inorganic Materials: Applied Research     Hybrid Journal   (Followers: 1)
Inorganica Chimica Acta     Hybrid Journal   (Followers: 7)
Inorganics     Open Access  
International Journal of Bio-Inorganic Hybrid Nanomaterials     Open Access   (Followers: 1)
International Journal of Inorganic Chemistry     Open Access   (Followers: 2)
JBIC Journal of Biological Inorganic Chemistry     Hybrid Journal   (Followers: 5)
Journal of Inorganic and Organometallic Polymers and Materials     Partially Free   (Followers: 9)
Journal of Inorganic Biochemistry     Hybrid Journal   (Followers: 6)
Journal of Polymer Engineering     Hybrid Journal   (Followers: 9)
Journal of Polymers and the Environment     Hybrid Journal   (Followers: 1)
Journal of Separation Science     Hybrid Journal   (Followers: 10)
Metallodrugs     Open Access   (Followers: 1)
Open Journal of Inorganic Chemistry     Open Access   (Followers: 2)
Plasmas and Polymers     Hybrid Journal  
Polymer Bulletin     Hybrid Journal   (Followers: 7)
Polymer Composites     Hybrid Journal   (Followers: 15)
Polyoxometalate Chemistry     Open Access  
Reviews in Inorganic Chemistry     Hybrid Journal  
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: 1)
Topics in Inorganic and General Chemistry     Full-text available via subscription  
Zeitschrift für anorganische und allgemeine Chemie     Hybrid Journal   (Followers: 2)
Zeitschrift für Kristallographie - New Crystal Structures     Open Access  
Journal Cover Journal of Inorganic Biochemistry
  [SJR: 0.983]   [H-I: 100]   [6 followers]  Follow
    
   Hybrid Journal Hybrid journal (It can contain Open Access articles)
   ISSN (Print) 0162-0134
   Published by Elsevier Homepage  [3031 journals]
  • Ruthenium(II) polypyridyl complexes: Synthesis, characterization and
           anticancer activity studies on BEL-7402 cells
    • Authors: Dan Wan; Shang-Hai Lai; Chuan-Chuan Zeng; Cheng Zhang; Bing Tang; Yun-Jun Liu
      Pages: 1 - 11
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Dan Wan, Shang-Hai Lai, Chuan-Chuan Zeng, Cheng Zhang, Bing Tang, Yun-Jun Liu
      Two new ligand PTTP (2-phenoxy-1,4,8,9-tetraazatriphenylene) and FTTP (2-(3-fluoronaphthalen-2-yloxy)-1,4,8,9-tetraazatriphenylene) and their six ruthenium(II) polypyridyl complexes [Ru(N-N)2(PTTP)](ClO4)2 and [Ru(N-N)2(FTTP)](ClO4)2 (N-N=dmb: 4,4′-dimethyl-2,2′-bipiridine; dmp: 2,9-dimethyl-1,10-phenanthroline; ttbpy: 4,4′-ditertiarybutyl-2,2′-bipyridine) were synthesized and characterized. The cytotoxic activity of the complexes against cancer cells HeLa, BEL-7402, A549, HepG-2, HOS and normal cell LO2 was evaluated by MTT method. The IC50 values range from 1.5±0.1 to 55.9±7.5μM. Complex 3 shows the highest cytotoxic activity toward BEL-7402 cells (IC50 =1.5±0.1μM). Complex 5 displays most effective inhibition of the cell growth in A549 and HOS cells with low IC50 values of 2.5±0.6 and 2.6±0.1μM, respectively. The apoptosis, reactive oxygen species, mitochondrial membrane potential, DNA damage, autophagy and anti-metastasis assay were investigated under a fluorescent microscope. The cell cycle arrest was assayed by flow cytometry, and the expression of caspases and Bcl-2 family proteins was studied by western blot. The results obtained show that the complexes induce apoptosis in BEL-7402 cells through a ROS-mediated mitochondrial dysfunction pathway.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.026
      Issue No: Vol. 173 (2017)
       
  • Arylsulfanyl groups - Suitable side chains for 5-substituted
           1,10-phenanthroline and nickel complexes as G4 ligands and telomerase
           inhibitors
    • Authors: Wanbo Liu; Siwen Wang; Irina A. Dotsenko; Vyacheslav V. Samoshin; Liang Xue
      Pages: 12 - 20
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Wanbo Liu, Siwen Wang, Irina A. Dotsenko, Vyacheslav V. Samoshin, Liang Xue
      Guanine-rich DNA sequences can undergo self-assembly into unique G-quadruplex structures that interfere with the binding of proteins to the same DNA region. The formation of DNA G-quadruplexes requires monovalent cations (Na+ and K+) or small molecules known as G-quadruplex (G4) ligands. Phenanthroline is a type of G4 ligand scaffold known for its coordination with metal ions to form complexes with a large aromatic surface area, which aptly stack with G-quartets. In this report, we have investigated the side chain effect on G-quadruplex recognition by evaluating a series of 5-substituted phenanthroline-based metal complexes (Phen-Ni) binding to telomeric G-quadruplex DNA. Results from biophysical methods including fluorescence and circular dichroism (CD) thermal denaturation, CD titration, and the fluorescent intercalator displacement (FID) assay suggest that several Phen-Ni complexes bind to G-quadruplex DNA with submicromolar G4DC50 values. Arylsulfanyl groups at the 5 position of 1,10-phenanthroline are the best side chains regarding binding affinity and selectivity towards G-quadruplex DNA. Most of the G-quadruplex binding Phen-Ni complexes can inhibit telomerase activity in vitro as indicated by the telomeric repeat amplification protocol (TRAP) assay and such inhibition is clearly concentration dependent. Our results here provide a guidance of utilizing 5-substituted phenanthroline derivatives as a viable and facile approach to design novel G4 ligands.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.018
      Issue No: Vol. 173 (2017)
       
  • Structural insights into the binding of buckwheat glutaredoxin with GSH
           and regulation of its catalytic activity
    • Authors: Xinyu Zhang; Wenming Wang; Chen Li; Yi Zhao; Hong Yuan; Xianshi Tan; Lijie Wu; Zhuanhua Wang; Hongfei Wang
      Pages: 21 - 27
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Xinyu Zhang, Wenming Wang, Chen Li, Yi Zhao, Hong Yuan, Xianshi Tan, Lijie Wu, Zhuanhua Wang, Hongfei Wang
      Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.019
      Issue No: Vol. 173 (2017)
       
  • Reaction mechanism of sterol hydroxylation by steroid C25 dehydrogenase
           – Homology model, reactivity and isoenzymatic diversity
    • Authors: Agnieszka Rugor; Anna Wójcik-Augustyn; Ewa Niedzialkowska; Stefan Mordalski; Jakub Staroń; Andrzej Bojarski; Maciej Szaleniec
      Pages: 28 - 43
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Agnieszka Rugor, Anna Wójcik-Augustyn, Ewa Niedzialkowska, Stefan Mordalski, Jakub Staroń, Andrzej Bojarski, Maciej Szaleniec
      Steroid C25 dehydrogenase (S25DH) is a molybdenum-containing oxidoreductase isolated from the anaerobic Sterolibacterium denitrificans Chol-1S. S25DH is classified as ‘EBDH-like’ enzyme (EBDH, ethylbenzene dehydrogenase) and catalyzes the introduction of an OH group to the C25 atom of a sterol aliphatic side-chain. Due to its regioselectivity, S25DH is proposed as a catalyst in production of pharmaceuticals: calcifediol or 25-hydroxycholesterol. The aim of presented research was to obtain structural model of catalytic subunit α and investigate the reaction mechanism of the O2-independent tertiary carbon atom activation. Based on homology modeling and theoretical calculations, a S25DH α subunit model was for the first time characterized and compared to other S25DH-like isoforms. The molecular dynamics simulations of the enzyme-substrate complexes revealed two stable binding modes of a substrate, which are stabilized predominantly by van der Waals forces in the hydrophobic substrate channel. However, H-bond interactions involving polar residues with C3=O/C3-OH in the steroid ring appear to be responsible for positioning the substrate. These results may explain the experimental kinetic results which showed that 3-ketosterols are hydroxylated 5–10-fold faster than 3-hydroxysterols. The reaction mechanism was studied using QM:MM and QM-only cluster models. The postulated mechanism involves homolytic CH cleavage by the MoO ligand, giving rise to a radical intermediate with product obtained in an OH rebound process. The hypothesis was supported by kinetic isotopic effect (KIE) experiments involving 25,26,26,26-[2H]-cholesterol (4.5) and the theoretically predicted intrinsic KIE (7.0–7.2). Finally, we have demonstrated that the recombinant S25DH-like isoform catalyzes the same reaction as S25DH.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.027
      Issue No: Vol. 173 (2017)
       
  • Speciation of potential anti-diabetic vanadium complexes in real serum
           samples
    • Authors: Daniele Sanna; Valeria Ugone; Maria Serra; Eugenio Garribba
      Pages: 52 - 65
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Daniele Sanna, Valeria Ugone, Maria Serra, Eugenio Garribba
      In this work the speciation in real serum samples of five VIVO complexes with potential application in the therapy of diabetes was studied through EPR spectroscopy as a function of V concentration (45.4, 90.9 and 454.5μM) and time (0–180min). [VO(dhp)2], [VO(ma)2], [VO(acac)2], [VO(pic)2(H2O)], and [VO(mepic)2], where Hdhp indicates 1,2-dimethyl-3-hydroxy-4(1H)-pyridinone, Hma maltol, Hacac acetylacetone, Hpic picolinic acid, and Hmepic 6-methylpicolinic acid, were examined. The distribution of VIVO2+ among the serum bioligands was calculated from the thermodynamic stability constants in the literature and compared with the experimental results. EPR results, which confirm the prediction, depend on the strength of the ligand L and geometry assumed by the bis-chelated species at physiological pH, cis-octahedral or square pyramidal. With dhp, the strongest chelator, the system is dominated by [VO(dhp)2] and/or cis-VO(dhp)2(Protein); with intermediate strength chelators, i.e. maltolate, acetylacetonate and picolinate, by cis-VO(ma)2(Protein), [VO(acac)2] or [VO(pic)(citrH−1)]3–−/[VO(pic)(lactH−1)]− (citr=citrate and lact=lactate) when the V concentration overcomes 100–200μM and by (VO)(hTf)/(VO)2(hTf) when concentration is lower than 100μM; with the weakest chelator, 6-methylpicolinate, (VO)(hTf)/(VO)2(hTf), (VO)(HSA) (hTf = human serum transferrin and HSA = human serum albumin), and VO(mepic)(Protein)(OH) are the major species at concentration higher than 100–200μM, whereas hydrolytic processes are observed for lower concentrations. For [VO(dhp)2], [VO(ma)2], [VO(acac)2] and [VO(pic)2(H2O)], the EPR spectra remain unaltered with elapsing time, while for mepic they change significantly because the hydrolyzed VIVO species are complexed by the serum bioligands, in particular by lactate. The rate of oxidation in the serum is [VO(dhp)2]>[VO(ma)2]>[VO(acac)2] and reflects the order of E 1/2 values.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.04.023
      Issue No: Vol. 173 (2017)
       
  • Antarctic fish versus human cytoglobins – The same but yet so
           different
    • Authors: Bert Cuypers; Stijn Vermeylen; Dietmar Hammerschmid; Stanislav Trashin; Vanoushe Rahemi; Albert Konijnenberg; Amy De Schutter; C.-H. Christina Cheng; Daniela Giordano; Cinzia Verde; Karolien De Wael; Frank Sobott; Sylvia Dewilde; Sabine Van Doorslaer
      Pages: 66 - 78
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Bert Cuypers, Stijn Vermeylen, Dietmar Hammerschmid, Stanislav Trashin, Vanoushe Rahemi, Albert Konijnenberg, Amy De Schutter, C.-H. Christina Cheng, Daniela Giordano, Cinzia Verde, Karolien De Wael, Frank Sobott, Sylvia Dewilde, Sabine Van Doorslaer
      The cytoglobins of the Antarctic fish Chaenocephalus aceratus and Dissostichus mawsoni have many features in common with human cytoglobin. These cytoglobins are heme proteins in which the ferric and ferrous forms have a characteristic hexacoordination of the heme iron, i.e. axial ligation of two endogenous histidine residues, as confirmed by electron paramagnetic resonance, resonance Raman and optical absorption spectroscopy. The combined spectroscopic analysis revealed only small variations in the heme-pocket structure, in line with the small variations observed for the redox potential. Nevertheless, some striking differences were also discovered. Resonance Raman spectroscopy showed that the stabilization of an exogenous heme ligand, such as CO, occurs differently in human cytoglobin in comparison with Antarctic fish cytoglobins. Furthermore, while it has been extensively reported that human cytoglobin is essentially monomeric and can form an intramolecular disulfide bridge that can influence the ligand binding kinetics, 3D modeling of the Antarctic fish cytoglobins indicates that the cysteine residues are too far apart to form such an intramolecular bridge. Moreover, gel filtration and mass spectrometry reveal the occurrence of non-covalent multimers (up to pentamers) in the Antarctic fish cytoglobins that are formed at low concentrations. Stabilization of these oligomers by disulfide-bridge formation is possible, but not essential. If intermolecular disulfide bridges are formed, they influence the heme-pocket structure, as is shown by EPR measurements.
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      PubDate: 2017-05-16T19:29:30Z
      DOI: 10.1016/j.jinorgbio.2017.04.025
      Issue No: Vol. 173 (2017)
       
  • Triphenyltin(IV) benzoates with diazenyl/imino scaffold exhibiting
           remarkable apoptosis mediated by reactive oxygen species
    • Authors: Tushar S. Basu Baul; Dhrubajyoti Dutta; Andrew Duthie; Ritika Prasad; Nishant Kumar Rana; Biplob Koch; Edward R.T. Tiekink
      Pages: 79 - 92
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Tushar S. Basu Baul, Dhrubajyoti Dutta, Andrew Duthie, Ritika Prasad, Nishant Kumar Rana, Biplob Koch, Edward R.T. Tiekink
      The cytotoxic potency of a series of triphenyltin(IV) compounds of general composition [Ph3Sn(Ln)] (1–6) has been probed in vitro employing MDA-MB-231 (human breast cancer) and HeLa (human cervical cancer) cell lines, where Ln =L1–3; isomeric 2/3/4-{(E)-2-[4-(dimethylamino)phenyl]diazenyl}benzoates and L4–6 are their corresponding isoelectronic imino analogues 2/3/4-[(E)-{[4-(dimethylamino)phenyl]methylidene}amino]benzoates. Compounds 1–6 have been characterized by elemental analysis and their spectroscopic properties were studied using IR and NMR (1H, 13C, 119Sn) techniques. The molecular structures of a pro-ligand 2-[(E)-{[4-(dimethylamino)phenyl]methylidene}amino]benzoic acid (HL4) and two representative molecules, Ph3Sn(L2) 2 and Ph3Sn(L5) 5, have been determined by X-ray crystallography. Structural analyses of 2 and 5 revealed distorted tetrahedral geometries within C3O donor sets owing to monodentate modes of coordination of the respective carboxylate ligands, close intramolecular Sn…O(carbonyl) interactions notwithstanding. Cytotoxic studies in vitro in MDA-MB-231 and HeLa cell lines revealed high activity, in sub-micromolar range, for all investigated compounds. Among these, 1 and 3 exhibited potent cytotoxicity most effectively towards MDA-MB-231 cells with a IC50 value of 1.19 and 1.44μM, respectively, whereas 5 showed remarkable activity towards HeLa cells with a IC50 value of 0.88μM, yet the series of compounds had minimal cytotoxic effect on normal HEK 293 (human embryonic kidney) cell line. The underlying investigation suggested that the compounds exert potent antitumor effect by elevating intracellular reactive oxygen species generation and cause delay in cell cycle by inhibiting cells at G2/M phase. The results presented herein suggest further development of this class of triphenyltin(IV) compounds-based drugs as potential anti-cancer therapies should be pursued.
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      PubDate: 2017-05-16T19:29:30Z
      DOI: 10.1016/j.jinorgbio.2017.04.020
      Issue No: Vol. 173 (2017)
       
  • Design, synthesis and evaluation of anticancer activity of ruthenium (II)
           polypyridyl complexes
    • Authors: Bing Tang; Dan Wan; Shang-Hai Lai; Hui-Hui Yang; Cheng Zhang; Xiu-Zhen Wang; Chuan-Chuan Zeng; Yun-Jun Liu
      Pages: 93 - 104
      Abstract: Publication date: Available online 10 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Bing Tang, Dan Wan, Shang-Hai Lai, Hui-Hui Yang, Cheng Zhang, Xiu-Zhen Wang, Chuan-Chuan Zeng, Yun-Jun Liu
      A new ligand PFPIP (PFPIP=2-(2,3,4,5,6-pentafluorophenyl)[4,5-f]imadazo [1,10]phenanthroline) and its four ruthenium(II) polypyridyl complexes [Ru(NN)2(PFPIP)](ClO4)2 (NN=dmb: 4,4′-dimethyl-2,2′-bipyridine, 1; bpy: 2,2′-bipyridine, 2; phen: 1,10-phenanthroline, 3; dmp: 2,9-dimethyl-1,10-phenanthroline, 4) were synthesized and characterized by elemental analysis, IR, 1H NMR, 13C NMR and ESI-MS. The cytotoxic activity in vitro of the ligand and complexes toward BEL-7402, A549, HeLa, HepG2 and MG-63 cell lines was evaluated using MTT method (MTT=(3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide). Complexes 1, 3 and 4 show moderate cytotoxic effect on the cell growth in BEL-7402 cells with IC50 values of 32.1±0.9, 37.9±1.7 and 42.1±3.0μM, respectively. The apoptosis in BEL-7402 cell was investigated with AO/EB and Hoechst 33,258 staining methods. The autophagy in BEL-7402 cell induced by complexes was assayed using MDC staining cell nuclei. The cell invasion, reactive oxygen species (ROS), mitochondrial membrane potential, cell cycle arrest, cellular uptake, comet assay and wound healing were studied under a fluorescent microscope. The complexes can cause autophagy and inhibit the cell invasion, and increase the ROS levels and induce a decrease in the mitochondrial membrane potential. The expression of the proteins related with apoptosis induced by the complexes was assayed by western blot analysis.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.04.028
      Issue No: Vol. 173 (2017)
       
  • Bis(diphenylphosphino)amines-containing ruthenium cymene complexes as
           potential anti-Mycobacterium tuberculosis agents
    • Authors: Juliana P. da Silva; Isabel C. Silva; Fernando R. Pavan; Davi F. Back; Márcio P. de Araujo
      Pages: 134 - 140
      Abstract: Publication date: August 2017
      Source:Journal of Inorganic Biochemistry, Volume 173
      Author(s): Juliana P. da Silva, Isabel C. Silva, Fernando R. Pavan, Davi F. Back, Márcio P. de Araujo
      Several ruthenium complexes have been investigated regarding anti-Mycobacterium tuberculosis (anti-MTb) activity, with some diphosphine-containing ruthenium complexes comparable to first and second line drugs. However, to the best of our knowledge, there is no PNP-containing ruthenium complexes applied as metallodrugs. Thus, this study focused on the synthesis, characterization and anti-MTb activity of a new series of coordination compounds with general formula [RuCl(η6-p-cymene)(PNR P)]X (R=CH2Py (Py=pyridine)− [1a], CH2Ph (Ph=phenyl)− [1b], Ph− [1c] and p-tol (p-tol= p-tolyl)− [1d]; X=PF6 − or BF4 −). The complexes were fully characterized by NMR (1H, 31P{1H}), vibrational spectroscopy (FTIR), ESI-MS, molar conductance, elemental analysis and X-ray diffraction studies. The molecular structures of [1a]PF 6 , [1c]BF 4 and [1d]PF 6 were determined and confirm the spectroscopic and ESI-MS data. The complexes were used in anti-MTb trials, and the preliminary results are presented. The complexes are promising anti-MTb agents with MIC90 (Minimum Inhibitory Concentration of compounds required to inhibit the growth of 90% of MTb) values comparable with the Ethambutol, the reference drug used in this work, and complex [1a]BF 4 presented the highest selectivity index.
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      PubDate: 2017-05-16T19:29:30Z
      DOI: 10.1016/j.jinorgbio.2017.04.008
      Issue No: Vol. 173 (2017)
       
  • A novel porphyrin-based molecular probe ZnTCPPSpm4 with catalytic,
           stabilizing and chiroptical diagnostic power towards DNA B-Z transition
    • Authors: Chiara M.A. Gangemi; Alessandro D'Urso; Gaetano A. Tomaselli; Nina Berova; Roberto Purrello
      Pages: 141 - 143
      Abstract: Publication date: Available online 14 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Chiara M.A. Gangemi, Alessandro D'Urso, Gaetano A. Tomaselli, Nina Berova, Roberto Purrello
      In this work we have designed a new zinc(II) porphyrin with four spermines conjugate in the meso positions, meso-tetrakis-(4-carboxysperminephenyl)porphyrin, ZnTCPPSpm4) with the aim of acting as a chiroptical probe for the Z-form of DNA, a high energy transient conformation of DNA. In addition to monitor by Electronic Circular Dichroism chiroptical response the formation of Z-DNA in the presence of micromolar concentration of spermine, this porphyrin based molecular probe is also able to catalyze and stabilize this important DNA structure. The ZnTCPPSpm4 conjugate represents a perfect example of single molecule, which possesses all these three properties at the same time. The increased stability of Z-DNA in the presence of this derivative opens possibility for further studies on the mechanism of B- to Z-DNA transition, and on the design of new probes with improved efficiency.
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      PubDate: 2017-05-16T19:29:30Z
      DOI: 10.1016/j.jinorgbio.2017.05.008
      Issue No: Vol. 173 (2017)
       
  • Design an anticancer copper(II) pro-drug based on the flexible IIA
           subdomain of human serum albumin
    • Authors: Yao Zhang; Zhenlei Zhang; Yi Gou; Ming Jiang; Hamid Khan; Zuping Zhou; Hong Liang; Feng Yang
      Pages: 1 - 8
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Yao Zhang, Zhenlei Zhang, Yi Gou, Ming Jiang, Hamid Khan, Zuping Zhou, Hong Liang, Feng Yang
      Owing to the flexible IIA sub-domain of human serum albumin (HSA), we proposed to rationally design a metal agent with a leaving group, and then regulate a leaving group of metal agent to be displaced by His-242 for improving its delivery efficiency and selectivity. To confirm our hypothesis, we synthesized a copper(II) compound derived from 2-amino-5-chlorophenol 2-hydroxybenzaldehyde Schiff-base, containing a leaving group [pyridine, PRD], namely Cu(L)(PRD). The HSA complex structure revealed that Cu(L)(PRD) binds to the hydrophobic cavity in HSA IIA sub-domain, His242 of HSA replaces the pyridine ligand in Cu compound, coordinating with Cu2+. HSA complex enhances cytotoxicity by about 1.4-fold in cancer cells but has no effect on normal cells in vitro through selectively accumulating into cancer cells. Interestingly, HSA complex has stronger anticancer capacity relative to unbound Cu(L)(PRD).
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.002
      Issue No: Vol. 172 (2017)
       
  • Rational design of dicarboxylato platinum(II) complexes with
           purine-mimetic ligands as novel anticancer agents
    • Authors: Kamil Hoffmann; Joanna Wiśniewska; Andrzej Wojtczak; Jerzy Sitkowski; Agnieszka Denslow; Joanna Wietrzyk; Mateusz Jakubowski; Iwona Łakomska
      Pages: 34 - 45
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Kamil Hoffmann, Joanna Wiśniewska, Andrzej Wojtczak, Jerzy Sitkowski, Agnieszka Denslow, Joanna Wietrzyk, Mateusz Jakubowski, Iwona Łakomska
      Six novel platinum(II) complexes containing purine-mimetic ligands (5,7-dimethyl-1,2,4-triazolo[1,5-a]pyrimidine (dmtp), 7-isobutyl-5-methyl-1,2,4-triazolo[1,5-a]pyrimidine (ibmtp), 5,7-ditertbutyl-1,2,4-triazolo[1,5-a]pyrimidine (dbtp)) and dicarboxylato ligands (glutarato (glut) or cyclobutane-1,1-dicarboxylato (CBDC)) have been prepared and characterized with multinuclear magnetic resonance (1H, 13C, 15N, 195Pt) NMR, infrared (IR) and X-ray crystallography. Spectroscopic data in solid state and in solution unambiguously confirm the square-planar geometry of Pt(II) with two monodentate N3-bonded 5,7-disubstituted-1,2,4-triazolo[1,5-a]pyrimidine ligands and one O-chelating dicarboxylato ligand. Next, the effect of all the platinum(II) compounds on the viability of normal or cancer cells and their putative mechanisms of action have been investigated. Of the studied platinum(II) complexes, two ([Pt(glut)(dbtp)2] and [Pt(CBDC)(dbtp)2]) overcame the cisplatin resistance in human ovarian tumor cells (A2780cis or OVCAR-3) and arrested the cell cycle at S phase in mice mammary gland cancer cells (4T1), which indicates a mechanism of action different from that of cisplatin. Interestingly, preliminary in vivo toxicity assays revealed that both compounds tested in mice ([Pt(glut)(dbtp)2] 3 and [Pt(CBDC)(dbtp)2] 6) were less toxic in vivo than cisplatin or oxaliplatin. Additionally, compound 6 did not cause myelosuppression and showed over fivefold less accumulation in the liver than its glutarato analog 3.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.003
      Issue No: Vol. 172 (2017)
       
  • In vitro antitumor activity, metal uptake and reactivity with ascorbic
           acid and BSA of some gold(III) complexes with N,N′-ethylenediamine
           bidentate ester ligands
    • Authors: Nebojša Pantelić; Bojana B. Zmejkovski; Branka Kolundžija; Marija Đorđić Crnogorac; Jelena M. Vujić; Biljana Dojčinović; Srećko R. Trifunović; Tatjana P. Stanojković; Tibor J. Sabo; Goran N. Kaluđerović
      Pages: 55 - 66
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Nebojša Pantelić, Bojana B. Zmejkovski, Branka Kolundžija, Marija Đorđić Crnogorac, Jelena M. Vujić, Biljana Dojčinović, Srećko R. Trifunović, Tatjana P. Stanojković, Tibor J. Sabo, Goran N. Kaluđerović
      Four novel gold(III) complexes of general formulae [AuCl2{(S,S)-R2eddl}]PF6 (R2eddl= O,O′-dialkyl-(S,S)-ethylenediamine-N,N′-di-2-(4-methyl)pentanoate, R= n-Pr, n-Bu, n-Pe, i-Bu; 1–4, respectively), were synthesized and characterized by elemental analysis, UV/Vis, IR, and NMR spectroscopy, as well as high resolution mass spectrometry. Density functional theory calculations pointed out that (R,R)-N,N′-configuration diastereoisomers were energetically the most favorable. Duo to high cytotoxic activity complex 3 was chosen for stability study in DMSO, no decomposition occurs within 24h, and for the reaction with ascorbic acid in which was reduced immediately. Additionally, 3 interacts with bovine serum albumin (BSA) as proven by UV/Vis spectroscopy. In vitro antitumor activity was determined against human cervix adenocarcinoma (HeLa), human myelogenous leukemia (K562), and human melanoma (Fem-x) cancer cell lines, as well as against non-cancerous human embryonic lung fibroblast cells MRC-5. The highest activity was observed against K562 cells (IC50: 5.04–6.51μM). Selectivity indices showed that these complexes are less toxic than cisplatin. 3 had a similar viability kinetics on HeLa cells as cisplatin. Drug accumulation studies in HeLa cells showed that the total gold uptake increased much faster than that of cisplatin pointing out that 3 more efficiently enters the cells than cisplatin. Furthermore, morphological and cell cycle analysis reveal that gold(III) complexes induced apoptosis in time- and dose-dependent manner.
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      PubDate: 2017-05-01T16:32:19Z
      DOI: 10.1016/j.jinorgbio.2017.04.001
      Issue No: Vol. 172 (2017)
       
  • Antimicrobial and anticancer photodynamic activity of a phthalocyanine
           photosensitizer with N-methyl morpholiniumethoxy substituents in
           non-peripheral positions
    • Authors: Jolanta Dlugaszewska; Wojciech Szczolko; Tomasz Koczorowski; Paulina Skupin-Mrugalska; Anna Teubert; Krystyna Konopka; Malgorzata Kucinska; Marek Murias; Nejat Düzgüneş; Jadwiga Mielcarek; Tomasz Goslinski
      Pages: 67 - 79
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Jolanta Dlugaszewska, Wojciech Szczolko, Tomasz Koczorowski, Paulina Skupin-Mrugalska, Anna Teubert, Krystyna Konopka, Malgorzata Kucinska, Marek Murias, Nejat Düzgüneş, Jadwiga Mielcarek, Tomasz Goslinski
      Photodynamic therapy involves the use of a photosensitizer that is irradiated with visible light in the presence of oxygen, resulting in the formation of reactive oxygen species. A novel phthalocyanine derivative, the quaternary iodide salt of magnesium(II) phthalocyanine with N-methyl morpholiniumethoxy substituents, was synthesized, and characterized. The techniques used included mass spectrometry (MALDI TOF), UV–vis, NMR spectroscopy, and photocytotoxicity against bacteria, fungi and cancer cells. The phthalocyanine derivative possessed typical characteristics of compounds of the phthalocyanine family but the effect of quaternization was observed on the optical properties, especially in terms of absorption efficiency. The results of the photodynamic antimicrobial effect study demonstrated that cationic phthalocyanine possesses excellent photodynamic activity against planktonic cells of both Gram-positive and Gram-negative bacteria. The bactericidal effect was dose-dependent and all bacterial strains tested were killed to a significant degree by irradiated phthalocyanine at a concentration of 1×10−4 M. There were no significant differences in the susceptibility of Gram-positive and Gram-negative bacteria to the applied photosensitizer. The photosensitivity of bacteria in the biofilm was lower than that in planktonic form. No correlation was found between the degree of biofilm formation and susceptibility to antimicrobial photodynamic inactivation. The anticancer activity of the novel phthalocyanine derivative was tested using A549 adenocarcinomic alveolar basal epithelial cells and the human oral squamous cell carcinoma cells derived from tongue (HSC3) or buccal mucosa (H413). No significant decrease in cell viability was observed under different conditions or with different formulations of the compound.
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      PubDate: 2017-05-01T16:32:19Z
      DOI: 10.1016/j.jinorgbio.2017.04.009
      Issue No: Vol. 172 (2017)
       
  • Chlorite reactivity with myoglobin: Analogy with peroxide and nitrite
           chemistry?
    • Authors: Cristina Bischin; Augustin Mot; Andrei Stefancu; Nicolae Leopold; Denisa Hathazi; Grigore Damian; Radu Silaghi-Dumitrescu
      Pages: 122 - 128
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Cristina Bischin, Augustin Mot, Andrei Stefancu, Nicolae Leopold, Denisa Hathazi, Grigore Damian, Radu Silaghi-Dumitrescu
      Stopped-flow UV–vis data allow for the first time direct spectroscopic detection of a ferryl species during the reaction of met myoglobin (Mb) with chlorite, analogous to what is observed in the reaction with peroxides. Ferryl is also observed in the reaction of oxy Mb+chlorite. A pathway involving Fe-O-O-ClO2 is explored by analogy with the Fe-O-O-NO and Fe-O-O-NO2 previously proposed as intermediates in the reactions of oxy globins with nitric oxide and nitrite, respectively. However, Fe-O-O-ClO2 is not detectable in these stopped-flow experiments and is in fact, unlike its nitrogenous congeners, predicted by density functional theory (DFT) to be impossible for a heme complex. Deoxy Mb reacts with chlorite faster than met – suggesting that, unlike with hydrogen peroxide (with which deoxy Mb reacts slower than met), binding of chlorite to the heme is not a rate-determining step (hence, most likely, an outer-sphere electron transfer mechanism); to correlate this, a Fe-O-Cl-O adduct was not observed experimentally for the met or for the deoxy reactions – even though prior DFT calculations suggest it to be feasible and detectable.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.017
      Issue No: Vol. 172 (2017)
       
  • Insights into signal transduction by a hybrid FixL: Denaturation study of
           on and off states of a multi-domain oxygen sensor
    • Authors: Wellinson G. Guimarães; Ana C.S. Gondim; Pedro Mikael da Silva Costa; Marie-Alda Gilles-Gonzalez; Luiz G.F. Lopes; Marta S.P. Carepo; Eduardo H.S. Sousa
      Pages: 129 - 137
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Wellinson G. Guimarães, Ana C.S. Gondim, Pedro Mikael da Silva Costa, Marie-Alda Gilles-Gonzalez, Luiz G.F. Lopes, Marta S.P. Carepo, Eduardo H.S. Sousa
      FixL from Rhizobium etli (ReFixL) is a hybrid oxygen sensor protein. Signal transduction in ReFixL is effected by a switch off of the kinase activity on binding of an oxygen molecule to ferrous heme iron in another domain. Cyanide can also inhibit the kinase activity upon binding to the heme iron in the ferric state. The unfolding by urea of the purified full-length ReFixL in both active pentacoordinate form, met-FixL(FeIII) and inactive cyanomet-FixL (FeIII-CN−) form was monitored by UV–visible absorption spectroscopy, circular dichroism (CD) and fluorescence spectroscopy. The CD and UV–visible absorption spectroscopy revealed two states during unfolding, whereas fluorescence spectroscopy identified a three-state unfolding mechanism. The unfolding mechanism was not altered for the active compared to the inactive state; however, differences in the ΔGH2O were observed. According to the CD results, compared to cyanomet-FixL, met-FixL was more stable towards chemical denaturation by urea (7.2 vs 4.8kJmol−1). By contrast, electronic spectroscopy monitoring of the Soret band showed cyanomet-FixL to be more stable than met-FixL (18.5 versus 36.2kJmol−1). For the three-state mechanism exhibited by fluorescence, the ΔGH2O for both denaturation steps were higher for the active-state met-FixL than for cyanomet-FixL. The overall stability of met-FixL is higher in comparison to cyanomet-FixL suggesting a more compact protein in the active form. Nonetheless, hydrogen bonding by bound cyanide in the inactive state promotes the stability of the heme domain. This work supports a model of signal transduction by FixL that is likely shared by other heme-based sensors.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.013
      Issue No: Vol. 172 (2017)
       
  • Novel copper(II) complexes with hydrazides and heterocyclic bases:
           Synthesis, structure and biological studies
    • Authors: Drielly A. Paixão; Ivana M. Marzano; Edgar H.L. Jaimes; Marcos Pivatto; Débora L. Campos; Fernando R. Pavan; Victor M. Deflon; Pedro Ivo da S. Maia; Ana M. Da Costa Ferreira; Isadora A. Uehara; Marcelo J.B. Silva; Françoise V. Botelho; Elene C. Pereira-Maia; Silvana Guilardi; Wendell Guerra
      Pages: 138 - 146
      Abstract: Publication date: July 2017
      Source:Journal of Inorganic Biochemistry, Volume 172
      Author(s): Drielly A. Paixão, Ivana M. Marzano, Edgar H.L. Jaimes, Marcos Pivatto, Débora L. Campos, Fernando R. Pavan, Victor M. Deflon, Pedro Ivo da S. Maia, Ana M. Da Costa Ferreira, Isadora A. Uehara, Marcelo J.B. Silva, Françoise V. Botelho, Elene C. Pereira-Maia, Silvana Guilardi, Wendell Guerra
      Five new copper(II) complexes of the type [Cu(NO)(NN)(ClO4)2], in which NO=4-fluorophenoxyacetic acid hydrazide (4-FH) or 4-nitrobenzoic hydrazide (4-NH) and NN=1,10-phenanthroline (phen), 4–4′-dimethoxy-2-2′-bipyridine (dmb) or 2,2-bipyridine (bipy) were synthesized and characterized using various spectroscopic methods. The X-ray structural analysis of one representative compound indicates that the geometry around the copper ion is distorted octahedron, in which the ion is coordinated to hydrazide via the terminal nitrogen and the carbonyl oxygen, and to heterocyclic bases via their two nitrogen atoms. Two perchlorate anions occupy the apical positions, completing the coordination sphere. The cytotoxic activity of compounds was investigated in three tumor cell lines (K562, MDA-MB-231 and MCF-7). Concerning K562 cell line, the complexes with 1,10-phenanthroline exhibit high cytotoxic activity and are more active than carboplatin, free ligands and [Cu(phen)2]2+. Considering the cytotoxicity results, further investigations for the compounds [Cu(4-FH)(phen)(ClO4)2] I and [Cu(4-NH)(phen)(ClO4)2]∙H2O III were performed. Flow cytometric analysis revealed that these complexes induce apoptotic cell death in MDA-MB-231 cell line and bind to DNA with K values of 4.38×104 and 2.62×104, respectively. These compounds were also evaluated against wild type Mycobacterium tuberculosis (ATCC 27294) and exhibited antimycobacterial activity, displayed MIC values lower than those of the corresponding free ligands.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.04.024
      Issue No: Vol. 172 (2017)
       
  • Synthesis, crystal structure and hydrolysis activity of a novel
           heterobinuclear cobalt(ІІІ) sodium(І) Schiff base complex
    • Authors: Xin Li; Zihui Liu; Ying Xu; Dongfeng Wang
      Pages: 37 - 44
      Abstract: Publication date: June 2017
      Source:Journal of Inorganic Biochemistry, Volume 171
      Author(s): Xin Li, Zihui Liu, Ying Xu, Dongfeng Wang
      A novel heterobinuclear complex [CoNa(C15H10NO4F)2(CH3OH)]2 with Schiff base (C15H10NO4F: 2-amino-4-fluorobenzoic acid-3-methoxysalicylaldehyde) was synthesized and characterized by IR and 1H NMR spectroscopy, elemental analysis and single crystal X-ray diffraction. X-ray crystallography reveals that the cobalt atom is six-coordinated by two nitrogen atoms from –CN–, two carboxylate oxygen atoms and two hydroxyl oxygen atoms in different ligands, while the sodium atom is seven-coordinated by two methoxy oxygen atoms, two hydroxyl oxygen atoms in different ligands, two oxygen atoms in the same carboxylate and one oxygen atom of solvent methanol. The reaction results of the complex with the p-nitrophenylphosphate (pNPP) and the adenosine monophosphate (AMP) reveal that the complex can hydrolyze phosphoester bonds. Then the DNA-hydrolysis activity is studied experimentally and theoretically, indicating that the complex can effectively hydrolyze the pBR322 supercoiled plasmid DNA. The molecular docking technology predicts the best binding site and binding affinity between the complex and DNA, and then the catalytic mechanism of hydrolysis is supposed. The study results suggest that the Schiff base metal complex, as a potent artificial enzyme, may find its applications in catalytic hydrolysis and biotechnological areas.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.03.005
      Issue No: Vol. 171 (2017)
       
  • A DFT/B3LYP study of the mechanisms of the O2 formation reaction catalyzed
           by the [(terpy)(H2O)MnIII(O)2MnIV(OH2)(terpy)](NO3)3 complex: A paradigm
           for photosystem II
    • Authors: Eduardo M. Sproviero
      Pages: 52 - 66
      Abstract: Publication date: June 2017
      Source:Journal of Inorganic Biochemistry, Volume 171
      Author(s): Eduardo M. Sproviero
      We present a theoretical study of the reaction pathway for dioxygen molecular formation catalyzed by the [(terpy)(H2O)MnIII(O)2MnIV(OH2) (terpy)](NO3)3 (terpy=2,2′:6′,2″-terpyridine) complex based on DFT-B3LYP calculations. In the initial state of the reaction, a partial oxido radical (0.44 spins) is formed ligated to Mn. This radical is involved in a nucleophylic attack by bulk water in the OO bond reaction formation step, in which the oxido fractional unpaired electron is delocalized toward the outermost Mn of the μ-oxo bridge, instead of the ligated Mn center. The reaction then follows with a series of proton-coupled electron transfer steps, in which the oxidation state, as well as the bond strength of the OO moiety increase, while the OOMn(1) bond gets weaker until O2 is released. In this model, basic acetate ions from the buffer solution capture protons in the proton-transfer steps. In each step there is reduction of the OOMn(1) binding strength, with concomitant increase of the OO bond strength, which culminates with the release of O2 in the last step. This last step is entropy driven, while formation of hydroperoxide and superoxide moieties is enthalpy driven. According with experiments, the rate-limiting step is the double oxidation of Mn(IV,III) or peroxymonosulfate binding, which occur prior to the OO bond formation step. This supports our findings that the barriers of all intermediate steps are below the experimental barrier of 19–21kcal/mol. The implications of these findings for understanding photosynthetic water-splitting catalysis are also discussed.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.02.014
      Issue No: Vol. 171 (2017)
       
  • Modulation effect of acidulated human serum albumin on Cu2+-mediated
           amyloid β-protein aggregation and cytotoxicity under a mildly acidic
           condition
    • Authors: Baolong Xie; Fufeng Liu; Xiaoyan Dong; Yongjian Wang; Xiaoguang Margaret Liu; Yan Sun
      Pages: 67 - 75
      Abstract: Publication date: June 2017
      Source:Journal of Inorganic Biochemistry, Volume 171
      Author(s): Baolong Xie, Fufeng Liu, Xiaoyan Dong, Yongjian Wang, Xiaoguang Margaret Liu, Yan Sun
      Aggregation of amyloid β-proteins (Aβ) induced by Cu2+ is a crucial element in the pathogenesis of Alzheimer's disease (AD), and cerebral acidosis is a common complication of AD. Under mildly acidic conditions, Cu2+-Aβ species have higher tendency to generate neurotoxic aggregates. Hence it is of significance to develop potent agents that inhibit Cu2+-mediated Aβ aggregation under a mildly acidic condition. Herein we synthesized acidulated human serum albumin (A-HSA) to mitigate Cu2+-mediated Aβ42 aggregation and cytotoxicity at pH6.6. Extensive experiments showed that A-HSA altered the pathway of Cu2+-mediated Aβ42 aggregation and protected SH-SY5Y cells from cytotoxicity and oxidative damage induced by Cu2+-Aβ42 species. Equimolar A-HSA increased cell viability from 52% to 91% as compared to Cu2+-Aβ42-treated group. Stopped-flow fluorescence analysis revealed that A-HSA changed the Cu2+-Aβ42 coordination mode from component I to II on the second timescale at pH6.6, which avoided the formation of aggregation-prone Cu2+-Aβ42 aggregates. The findings revealed that the more negative charges on A-HSA surface could stabilize the protonated form of the adjacent histidine residues of Aβ42. Hence, component I, which is necessary to form toxic aggregates, became unstable in the presence of A-HSA. On the other hand, hydrophobic binding and electrostatic repulsion could work simultaneously on the bound Aβ42 on A-HSA surface. The two opposite forces stretched Aβ42 conformations, which inhibited the formation of toxic Cu2+-Aβ42 aggregates. Thus, A-HSA worked as a bifunctional inhibitor against Cu2+-mediated Aβ42 aggregation and cytotoxicity under a mildly acidic condition.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.03.009
      Issue No: Vol. 171 (2017)
       
  • Characterization of tRNALeu binding interactions with Cu2+ and Pb2+ and
           their biological implications
    • Authors: Aleksandar Dimkovikj; Mallory J. Banton; Lance A. McDanel; Katelin N. Arndt; Katelyn E. Unvert; Elizabeth K. Thorn; Ana Royo Marco; Rachel A. Hellmann-Whitaker
      Pages: 90 - 99
      Abstract: Publication date: June 2017
      Source:Journal of Inorganic Biochemistry, Volume 171
      Author(s): Aleksandar Dimkovikj, Mallory J. Banton, Lance A. McDanel, Katelin N. Arndt, Katelyn E. Unvert, Elizabeth K. Thorn, Ana Royo Marco, Rachel A. Hellmann-Whitaker
      RNA is known to interact with Mg2+ when assuming higher-ordered tertiary configurations. Structurally, when tRNA molecules interact with Mg2+, they consistently form a “L-shape” conformation each time they are synthesized. Therefore, if Mg2+ can induce tertiary structure formation, then binding to alternative cations could produce alternative tertiary configurations. By utilizing circular dichroism and mobility gel-shift assays it was observed that tRNA structure can be altered when in the presence of different divalent cationic species. Formation of these alternative structural configurations was further validated by aminoacylating these tRNA structural anomalies with their native enzyme, which resulted in markedly different degrees of activity. Thus, it was confirmed that structural changes do occur when tRNA forms complexes with different cations. To better understand these structural changes, quantitative cation binding to tRNA was determined through titrations as well as ICP-OES analysis, which indicated that the metal ions can bind to the tRNA structure in specific and non-specific ways. Lastly, it was observed through stopped-flow kinetics that tRNA can associate/dissociate from different cations to varying degrees, thus forming cation-specific complexes at unique rates.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.03.008
      Issue No: Vol. 171 (2017)
       
  • Characteristics of minerals in vesicles produced by human osteoblasts hFOB
           1.19 and osteosarcoma Saos-2 cells stimulated for mineralization
    • Authors: Agnieszka Strzelecka-Kiliszek; Lukasz Bozycki; Saida Mebarek; Rene Buchet; Slawomir Pikula
      Pages: 100 - 107
      Abstract: Publication date: June 2017
      Source:Journal of Inorganic Biochemistry, Volume 171
      Author(s): Agnieszka Strzelecka-Kiliszek, Lukasz Bozycki, Saida Mebarek, Rene Buchet, Slawomir Pikula
      Bone cells control initial steps of mineralization by producing extracellular matrix (ECM) proteins and releasing vesicles that trigger apatite nucleation. Using transmission electron microscopy with energy dispersive X-ray microanalysis (TEM-EDX) we compared the quality of minerals in vesicles produced by two distinct human cell lines: fetal osteoblastic hFOB 1.19 and osteosarcoma Saos-2. Both cell lines, subjected to osteogenic medium with ascorbic acid (AA) and β-glycerophosphate (β-GP), undergo the entire osteoblastic differentiation program from proliferation to mineralization, produce the ECM and spontaneously release vesicles. We observed that Saos-2 cells mineralized better than hFOB 1.19, as probed by Alizarin Red-S (AR-S) staining, tissue nonspecific alkaline phosphatase (TNAP) activity and by analyzing the composition of minerals in vesicles. Vesicles released from Saos-2 cells contained and were surrounded by more minerals than vesicles released from hFOB 1.19. In addition, there were more F and Cl substituted apatites in vesicles from hFOB 1.19 than in those from Saos-2 cells as determined by ion ratios. Saos-2 and h-FOB 1.19 cells revealed distinct mineralization profiles, indicating that the process of mineralization may proceed differently in various types of cells. Our findings suggest that TNAP activity is correlated with the relative proportions of mineral-filled vesicles and mineral-surrounded vesicles. The origin of vesicles and their properties predetermine the onset of mineralization at the cellular level.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.03.006
      Issue No: Vol. 171 (2017)
       
  • Controlled self-assembling structures of ferrocene-dipeptide conjugates
           composed of Ala-Pro-NHCH2CH2SH dipeptide chain
    • Authors: Toshiyuki Moriuchi; Taiki Nishiyama; Yoshiki Tayano; Toshikazu Hirao
      Abstract: Publication date: Available online 18 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Toshiyuki Moriuchi, Taiki Nishiyama, Yoshiki Tayano, Toshikazu Hirao
      Bioorganometallic ferrocene-dipeptide conjugates with the Ala-Pro-cysteamine dipeptide chain, Fc-L-Ala-L-Pro-NHCH2CH2SH (2) and Fc-L-Ala-D-Pro-NHCH2CH2SH (4) (Fc=ferrocenoyl), were prepared by the reduction of the ferrocene-dipeptide conjugates, Fc-L-Ala-L-Pro-cystamine-L-Pro-L-Ala-Fc (1) or Fc-L-Ala-D-Pro-cystamine-D-Pro-L-Ala-Fc (3), respectively. Control of the self-assembling structures of ferrocene-dipeptide conjugates was demonstrated by changing the chirality of amino acids. The molecular structure of 2 composed of the L-Ala-L-Pro-NHCH2CH2SH dipeptide chain confirmed the formation of intramolecular hydrogen bond of N-H⋯N pattern between the NH of cysteamine moiety and the nitrogen of Pro moiety. Furthermore, intermolecular hydrogen bonds between NH (Ala) and CO (Pro of another molecule) and between NH (cysteamine) and CO (the ferrocenoyl moiety of another molecule) were formed, wherein each molecule is connected to four neighboring molecules by continuous intermolecular hydrogen bonds to form the hydrogen-bonded molecular assembling structure. On the contrary, the left-handed helical assembly through an intermolecular hydrogen-bonding network of 15-membered intermolecularly hydrogen-bonded ring between NH (Ala) and CO (the ferrocenoyl moiety of another molecule) and between NH (the cysteamine moiety of another molecule) and CO (Ala) was observed in the crystal packing of 4 composed of the L-Ala-D-Pro-NHCH2CH2SH dipeptide chain.
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      PubDate: 2017-05-21T19:54:25Z
      DOI: 10.1016/j.jinorgbio.2017.05.009
       
  • Photochemical studies of cis-[Ru(bpy)2(4-bzpy)(CO)](PF6)2 and
           cis-[Ru(bpy)2(4-bzpy)(Cl)](PF6): Blue light-induced nucleobase binding
    • Authors: Aurideia P. de Sousa; Edinilton M. Carvalho; Javier Ellena; Eduardo H.S. Sousa; Jackson R. de Sousa; Luiz G.F. Lopes; Peter C. Ford; Alda K.M. Holanda
      Abstract: Publication date: Available online 15 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Aurideia P. de Sousa, Edinilton M. Carvalho, Javier Ellena, Eduardo H.S. Sousa, Jackson R. de Sousa, Luiz G.F. Lopes, Peter C. Ford, Alda K.M. Holanda
      The ruthenium(II) compounds cis-[Ru(bpy)2(4-bzpy)(CO)](PF6)2 (I) and cis-[Ru(bpy)2(4-bzpy)(Cl)](PF6) (II) (4-bzpy=4-benzoylpyridine, bpy=2,2′-bipyridine) were synthesized and characterized by spectroscopic and electrochemical techniques. The crystal structure of II was determined by X-ray diffraction. The photochemical behavior of I in aqueous solution shows that irradiation with ultraviolet light (365nm) releases both CO and 4-bzpy leading to the formation of the cis-[Ru(bpy)2(H2O)2]2+ ion as identified by NMR and electronic spectroscopy. Carbon monoxide release was confirmed with the myoglobin method and by gas chromatographic analysis of the headspace. CO release was not observed when aqueous I was irradiated with blue light (453nm). Changes in the electronic and 1H NMR spectra indicate that I undergoes photoaquation of 4-bzpy to form cis-[Ru(bpy)2(CO)(H2O)]2+. Blue light irradiation of aqueous II released the coordinated 4-bzpy to give the cis-[Ru(bpy)2(H2O)(Cl)]2+ ion. When the latter reaction was carried out in the presence of the nucleobase guanine, Ru-guanine adducts were formed, indicating that the metal containing photoproduct may also participate in biologically relevant reactions. The photochemical behavior of I indicates that it can release either CO or 4-bzpy depending on the wavelength chosen, a feature that may have therapeutic application.
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      PubDate: 2017-05-16T19:29:30Z
      DOI: 10.1016/j.jinorgbio.2017.05.006
       
  • Structure-activity relationship between Zn2+-chelated alkylated
           poly(1-vinylimidazole) and gene transfection
    • Authors: Shoichiro Asayama; Mizuki Sakata; Hiroyoshi Kawakami
      Abstract: Publication date: Available online 10 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Shoichiro Asayama, Mizuki Sakata, Hiroyoshi Kawakami
      The structure-activity relationship between Zn2+-chelated alkylated poly(1-vinylimidazole) (PVIm) and gene transfection has been demonstrated. From a chemical structure perspective, ethylated PVIm (PVIm-Et) chelated the most Zn2+ ions compared to methylated PVIm (PVIm-Me) and butylated PVIm (PVIm-Bu). The resulting Zn2+-chelated PVIm-Et formed more stable complexes with plasmid DNA complex than non-chelated PVIm-Et. From a biological activity perspective, the Zn2+-chelated PVIm-Et delivered the highest amount of Zn2+ ions inside the cell, corresponding to the highest gene transfection. These results suggest that PVIm-Et is the optimal sequence for the chelation of Zn2+ ions to enhance the gene transfection activity. The structure-activity relationship in this study is expected to offer a unique molecular design for drug/gene delivery systems.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.05.007
       
  • Uptake of Ga-curcumin derivatives in different cancer cell lines: Toward
           the development of new potential 68Ga-labelled curcuminoids-based
           radiotracers for tumour imaging
    • Authors: Sara Rubagotti; Stefania Croci; Erika Ferrari; Giulia Orteca; Michele Iori; Pier C. Capponi; Annibale Versari; Mattia Asti
      Abstract: Publication date: Available online 10 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Sara Rubagotti, Stefania Croci, Erika Ferrari, Giulia Orteca, Michele Iori, Pier C. Capponi, Annibale Versari, Mattia Asti
      Thanks to the ability to suppress the proliferation and to kill tumour cells, several studies have shown the anti-cancer effects of curcumin (CUR) and its derivatives, i.e. diacetylcurcumin (DAC) and bis-dehydroxycurcumin (bDHC). This study is focused onto the development of curcuminoid complexes with gallium-68 employed as potential new radio-labelled probes to detect neoplastic tissues through imaging techniques such as positron emission tomography. To this purpose, the uptake of three Ga-curcuminoid complexes, namely Ga(CUR)2 +, Ga(DAC)2 +, Ga(bDHC)2 +, by various tumour cell lines was compared with the uptake of the same compounds by normal human lymphocytes by flow cytometry using the intrinsic fluorescence of the curcuminoids. Ga(CUR)2 +, and particularly Ga(DAC)2 +, showed a higher uptake by colorectal carcinoma (HT29) and lymphoma (K562) cell lines than lymphocytes, while the uptake of Ga(bDHC)2 + was higher in lymphocytes than in all the other cell lines. Based on the fluorescence data, Gallium-68 labelled complexes were then tested in HT29 cell line. 68Ga(DAC)2 + showed the highest uptake by HT29 cells (higher internalization with a lower externalization) and the highest affinity. The obtained results are promising and the findings foster further investigation on the development of curcumin-metal-based radiopharmaceuticals.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.05.002
       
  • A comparison study on RNase A oligomerization induced by cisplatin,
           carboplatin and oxaliplatin
    • Authors: Delia Picone; Federica Donnarumma; Giarita Ferraro; Giovanni Gotte; Andrea Fagagnini; Giovanna Butera; Massimo Donadelli; Antonello Merlino
      Abstract: Publication date: Available online 9 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Delia Picone, Federica Donnarumma, Giarita Ferraro, Giovanni Gotte, Andrea Fagagnini, Giovanna Butera, Massimo Donadelli, Antonello Merlino
      Cisplatin (CDDP) can form interprotein cross-links, leading to the formation of platinated oligomers. A dimer, a trimer and higher oligomers of bovine pancreatic ribonuclease (RNase A) obtained upon reaction with CDDP in 1:10 protein to metal ratio at 37°C have been previously characterized. Here, we verify the ability of carboplatin and oxaliplatin to induce RNase A oligomerization under the same experimental conditions. The amount of formed RNase A oligomers was compared with that obtained in the reaction of the protein with CDDP. Among the three anticancer agents, CDDP is the most reactive and the most effective in inhibiting the ribonucleolytic activity of the protein. Oxaliplatin is the least potent oligomerization agent. Biophysical characterizations of structure and stability of platinated dimers formed in the presence of carboplatin and oxaliplatin suggest that they have a similar thermal stability and are more prone to dissociation than the corresponding dimer obtained with CDDP. Oligomers obtained in the presence of carboplatin are the most active. X-ray structures of the monomeric adducts that RNase A forms with the three drugs provide a rational basis to explain the different effects of the three anticancer agents on enzymatic activity and protein aggregation. Although platinated oligomers of RNase A formed upon reaction with CDDP, carboplatin and oxaliplatin retain a residual ribonuclease activity, they do not show cytotoxic action, suggesting that protein aggregation processes induced by Pt-based drugs can represent a collateral drawback, which affects the functional state of protein targets and reduces the efficacy of Pt-based drug treatment.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.05.005
       
  • Competitive reactions among glutathione, cisplatin and
           copper-phenanthroline complexes
    • Authors: Enzo Cadoni; Elisa Valletta; Graziano Caddeo; Francesco Isaia; Maria Grazia Cabiddu; Sarah Vascellari; Tiziana Pivetta
      Abstract: Publication date: Available online 8 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Enzo Cadoni, Elisa Valletta, Graziano Caddeo, Francesco Isaia, Maria Grazia Cabiddu, Sarah Vascellari, Tiziana Pivetta
      A large number of cancers are treated with cisplatin (CDDP). However, its use is limited by drug resistance, which is often related to intracellular levels of thiol-containing molecules such as glutathione (GSH). The role of GSH in cisplatin-resistant cancer cells is still unclear. GSH may form adducts with CDDP which results in the deactivation of the drug, and, actually, a high intracellular level of GSH was observed in some cisplatin-resistant cancers. To overcome drug resistance, CDDP is often administered in combination with one or more drugs to exploit a possible synergistic effect. In previous studies, we observed that the sensitivity to CDDP of leukemic and ovarian cisplatin-resistant cancer cells was restored in the presence of [Cu(phen)2(H2O)](ClO4)2 (C0) (phen is 1,10-phenathroline). In order to clarify the possible interactions between GSH and CDDP, the reactivity and competitive reactions among CDDP, C0 and GSH in binary and ternary mixtures were studied. The investigation was extended also to [Cu(phen)(H2O)2(ClO4)2] (C10) and GSSG, the oxidized form of GSH. It was observed that CDDP was able to react with the studied copper complexes and with GSH or GSSG. However, in mixtures containing CDDP, GSH or GSSG and C0 or C10, only copper-glutathione complexes were detected, while no platinum-glutathione adducts were found.
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      PubDate: 2017-05-11T19:13:03Z
      DOI: 10.1016/j.jinorgbio.2017.05.004
       
  • DNA and protein binding, double-strand DNA cleavage and cytotoxicity of
           mixed ligand copper(II) complexes of the antibacterial drug nalidixic acid
           
    • Authors: Rangasamy Loganathan; Mani Ganeshpandian; Nattamai S.P. Bhuvanesh; Mallayan Palaniandavar; Amsaveni Muruganantham; Swapan K. Ghosh; Anvarbatcha Riyasdeen; Mohammad Abdulkader Akbarsha
      Abstract: Publication date: Available online 3 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Rangasamy Loganathan, Mani Ganeshpandian, Nattamai S.P. Bhuvanesh, Mallayan Palaniandavar, Amsaveni Muruganantham, Swapan K. Ghosh, Anvarbatcha Riyasdeen, Mohammad Abdulkader Akbarsha
      The water soluble mixed ligand complexes [Cu(nal)(diimine)(H2O)](ClO4) 1–4, where H(nal) is nalidixic acid and diimine is 2,2′-bipyridine (1), 1,10-phenanthroline (2), 5,6-dimethyl-1,10-phenanthroline (3), and 3,4,7,8-tetramethyl-1,10-phenanthroline (4), have been isolated. The coordination geometry around Cu(II) in 1 and that in the Density Functional Theory optimized structures of 1–4 has been assessed as square pyramidal. The trend in DNA binding constants (K b) determined using absorption spectral titration (K b: 1, 0.79±0.1< 2, 1.06±0.1< 3, 1.79±0.2< 4, 1.84±0.2×105 M−1) is in line with that (K app) determined by competitive ethidium bromide binding studies. The large red-shift (10nm) observed for 2 suggests that the phen co-ligand is stacked with a frayed DNA base pair. In contrast, 3 and 4 are involved in intimate hydrophobic interaction with DNA through the methyl substituents on phen ring, which is supported by viscosity and protein binding studies. DNA docking studies imply that 4 is involved preferentially in DNA major groove binding while 1–3 in minor groove binding and that all the complexes, upon removing the axially coordinated water molecule, bind in the major groove. Interestingly, 3 and 4 display prominent double-strand DNA cleavage while 1 and 2 effect only single-strand DNA cleavage in the absence of an activator. The complexes 3 and 4 show cytotoxicity higher than 1 and 2 against human breast cancer cell lines (MCF-7). The complex 4 induces apoptotic mode of cell death in cancer cells.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.05.001
       
  • Prediction of ligand effects in platinum-amyloid-β coordination
    • Authors: Matthew Turner; Robert J. Deeth; James A. Platts
      Abstract: Publication date: Available online 2 May 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Matthew Turner, Robert J. Deeth, James A. Platts
      Ligand field molecular mechanics (LFMM) and semi-empirical Parametric Model 7 (PM7) methods are applied to a series of six PtII-Ligand systems binding to the N-terminal domain of the amyloid-β (Aβ) peptide. Molecular dynamics using a combined LFMM/Assisted Model Building with Energy Refinement (AMBER) approach is used to explore the conformational freedom of the peptide fragment, and identifies favourable platinum binding modes and peptide conformations for each ligand investigated. Platinum coordination is found to depend on the nature of the ligand, providing evidence that binding mode may be controlled by suitable ligand design. Boltzmann populations at 310K indicate that each Pt-Aβ complex has a small number of thermodynamically accessible states. Ramachandran maps are constructed for the sampled Pt-Aβ conformations and secondary structural analysis of the obtained complex structures is performed and contrasted with the free peptide; coordination of these platinum complexes disrupts existing secondary structure in the Aβ peptide and promotes formation of ligand-specific turn-type secondary structure.
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      PubDate: 2017-05-06T18:42:12Z
      DOI: 10.1016/j.jinorgbio.2017.05.003
       
  • Copper(II) and iron(III) ions inhibit respiration and increase
           free-radical mediated phospholipid peroxidation in rat liver mitochondria:
           Effect of antioxidants
    • Authors: Christian Saporito-Magriñá; Rosario Musacco-Sebio; Juan M. Acosta; Sofía Bajicoff; Paola Paredes-Fleitas; Sofia Reynoso; Alberto Boveris; Marisa G. Repetto
      Abstract: Publication date: Available online 19 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Christian Saporito-Magriñá, Rosario Musacco-Sebio, Juan M. Acosta, Sofía Bajicoff, Paola Paredes-Fleitas, Sofia Reynoso, Alberto Boveris, Marisa G. Repetto
      Rat liver mitochondria (1.5–2.1mg protein·mL−1) supplemented with either 25 and 100μM Cu2+ or 100 and 500μM Fe3+ show inhibition of active respiration (O2 consumption in state 3) and increased phospholipid peroxidation . Liver mitochondria were supplemented with the antioxidants reduced glutathione, N-acetylcysteine or butylated hydroxitoluene, to evaluate their effects on the above-mentioned alterations. Although the mitochondrial dysfunction is clearly associated to phospholipid peroxidation, the different responses to antioxidant supplementation indicate that the metal ions have differences in their mechanisms of toxicity. Mitochondrial phospholipid peroxidation through the formation of hydroxyl radical by a Fenton/Haber-Weiss mechanism seems to precede the respiratory inhibition and to be the main fact in Fe-induced mitochondrial dysfunction. In the case of Cu2+, it seems that the ion oxidizes glutathione, and low molecular weight protein thiol groups in a direct reaction, as part of its intracellular redox cycling. The processes involving phospholipid peroxidation, protein oxidation and mitochondrial respiratory inhibition characterize a redox dyshomeostatic situation that ultimately leads to cell death. However, Cu2+ exposure involves an additional, yet unidentified, toxic event as previous reduction of the metal with N-acetylcysteine has only a minor effect in preventing the mitochondrial damage.
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      PubDate: 2017-04-24T16:15:50Z
      DOI: 10.1016/j.jinorgbio.2017.04.012
       
  • Synthesis, structure and cytotoxicity of a series of Dioxidomolybdenum(VI)
           complexes featuring Salan ligands
    • Authors: Satabdi Roy; Monalisa Mohanty; Sagarika Pasayat; Sudarshana Majumder; Kulanthaivel Senthilguru; Indranil Banerjee; Martin Reichelt; Hans Reuter; Ekkehard Sinn; Rupam Dinda
      Abstract: Publication date: Available online 18 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Satabdi Roy, Monalisa Mohanty, Sagarika Pasayat, Sudarshana Majumder, Kulanthaivel Senthilguru, Indranil Banerjee, Martin Reichelt, Hans Reuter, Ekkehard Sinn, Rupam Dinda
      Seven hexacoordinated cis-dioxidomolybdenum(VI) complexes [MoO2L1–7] (1–7) derived from various tetradentate diamino bis(phenolato) “salan” ligands, N,N′-dimethyl-N,N′-bis-(2-hydroxy-3-X-5-Y-6-Z-benzyl)-1,2-diaminoethane {(X=Br, Y=Me, Z=H (H2L1); X=Me, YCl, Z=H (H2L2); X= iPr, Y=Cl, Z=Me (H2L3)} and N,N′-bis-(2-hydroxy-3-X–5-Y-6-Z-benzyl)-1,2-diaminopropane {(X=Y= tBu, Z=H (H2L4); X=Y=Me, Z=H (H2L5); X= iPr, YCl, Z=Me (H2L6); X=Y=Br, Z=H (H2L7)} containing ON donor atoms, have been isolated and structurally characterized. The formation of cis-dioxidomolybdenum(VI) complexes was confirmed by elemental analysis, IR, UV–vis and NMR spectroscopy, ESI-MS and cyclic voltammetry. X-ray crystallography showed the O2N2 donor set to define an octahedral geometry in each case. The complexes (1–7) were tested for their in vitro antiproliferative activity against HT-29 and HeLa cancer cell line. IC50 values of the complexes in HT-29 follow the order 6 < 7 << 1 < 2 < 5 << 3 < 4 while the order was 6 < 7 < 5 < 1 << 3 < 4 < 2 in HeLa cells. Some of the complexes proved to be as active as the clinical referred drugs, and the greater potency of 6 and 7 (IC50 values of 6 are 2.62 and 10.74μM and that of 7 is 11.79 and 30.48μM in HT-29 and HeLa cells, respectively) may be dependent on the substituents in the salan ligand environment coordinated to the metal.
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      PubDate: 2017-04-24T16:15:50Z
      DOI: 10.1016/j.jinorgbio.2017.04.015
       
  • Ferrocenyl and organic novobiocin derivatives: Synthesis and their in
           vitro biological activity
    • Authors: Mziyanda Mbaba; Amanda N. Mabhula; Natasha Boel; Adrienne L. Edkins; Michelle Isaacs; Heinrich C. Hoppe; Setshaba D. Khanye
      Abstract: Publication date: Available online 13 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Mziyanda Mbaba, Amanda N. Mabhula, Natasha Boel, Adrienne L. Edkins, Michelle Isaacs, Heinrich C. Hoppe, Setshaba D. Khanye
      A focused series of novobiocin derivatives containing a ferrocene unit together with their corresponding organic novobiocin analogues have been synthesized in modest to good yields. These compounds were screened for biological activity against a chloroquine-sensitive strain of Plasmodium falciparum (3D7) and human breast cancer cell line (HCC38). With the exception of compounds 5c and 5d, the general trend observed is that incorporation of the ferrocene moiety into novobiocin scaffold resulted in compounds 6a–d/6f showing enhanced activity compared to organic analogues 5a–b and 5e–f.
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      PubDate: 2017-04-17T15:43:03Z
      DOI: 10.1016/j.jinorgbio.2017.04.014
       
  • Study on electronic properties, thermodynamic and kinetic parameters of
           the selected platinum(II) derivatives interacting with guanine
    • Authors: Filip Šebesta; Jaroslav V. Burda
      Abstract: Publication date: Available online 12 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Filip Šebesta, Jaroslav V. Burda
      Interaction of hydrated forms of several potential anticancer agents (PtCl2(diaminocyclohexane), trans-[PtCl2(NH3)(thiazole)], cis-[PtCl2(NH3)(piperidine)], and cis-PtCl2(NH3)(cyclohexylamine) complexes) with guanine are explored and compared with an analogous interaction of cisplatin. Basic electronic properties, binding and stabilization energies are determined and energy profiles for the aquation reaction are estimated at the B3LYP/6-311++G(2df,2pd) level of theory. It is found that the substitution reaction is an exothermic and exergonic process with ΔG slightly less negative than −20kcal/mol. The largest energy release occurs for PtCl(H2O)(diaminocyclohexane) complex. The rate constants for the Pt(II) complexes in the chloro- and hydroxo-form are compared and an impact of the ligand in the trans position to water is discussed.
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      PubDate: 2017-04-17T15:43:03Z
      DOI: 10.1016/j.jinorgbio.2017.04.006
       
  • Development and applications of two colorimetric and fluorescent
           indicators for Hg2+ detection
    • Authors: Ying Long; Mei-pan Yang; Bing-qin Yang
      Abstract: Publication date: Available online 9 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Ying Long, Mei-pan Yang, Bing-qin Yang
      Two rhodamine-active probes RBAI (Rhodamine B-di-Aminobenzene-phenyl Isothiocyanate) and RGAI (Rhodamine 6G-di-Aminobenzene-phenyl Isothiocyanate) were designed, synthesized and characterized. The probes were developed as fluorescent and colorimetric chemodosimeters in ethanol-water solution with a broad pH span (5–10) and high selectivity toward Hg2+ but no significant response toward other common competitive cations. The Hg2+-promoted ring opening of spirolactam of the rhodamine moiety induced cyclic guanylation of the thiourea moiety, which resulted in the dual chromo- and fluorogenic observation (off-on). Cytotoxicity and bioimaging studies by L929 living cells and living mice indicated that the probes were negligible cytotoxicity, cell permeable and suitable for detecting Hg2+ in biological environments. Moreover, the new probes not only displayed excellent abilities for the successful detection of Hg2+ in L929 living cells and living mice but also able to detect Hg2+ by adsorbing on solid surfaces and quantitative detection of Hg2+ in real water samples with good recovery (more than 90%), indicating that they have promising prospect for application for Hg2+ sensing in environmental and biological sciences.
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.010
       
  • Three phases in pH dependent heme abstraction from myoglobin
    • Authors: Sohini Mukherjee; Manjistha Mukherjee; Sabyasachi Bandyopadhyay; Abhishek Dey
      Abstract: Publication date: Available online 9 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Sohini Mukherjee, Manjistha Mukherjee, Sabyasachi Bandyopadhyay, Abhishek Dey
      The extent of heme extraction from myoglobin (Mb) by methylethyl ketone is found to be pH dependent and show three distinct phases. Parallel investigations of the protein using resonance Raman (rR) and circular dichroism (CD) across these pH regions indicate that these phases correspond to three different protonation steps in holoMb as the pH of the solution changed. The first transition occurs between pH5–6 and is due to the protonation of one of the heme propionate groups which disrupts its H-bonding with Arg 45 in the loop. The 2nd phase (pH5–4) likely involves the protonation of the 2nd propionate which H-bonds to Ser 92 in the F-helix. The third phase (pH<3.5) involves dissociation of the FeII His bond which eventually leads to complete heme dissociation and unfolding.
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.011
       
  • Enzymatic activity of the CaM-PDE1 system upon addition of actinyl ions
    • Authors: Florian Brulfert; Samir Safi; Aurélie Jeanson; Harald Foerstendorf; Stephan Weiss; Catherine Berthomieu; Sandrine Sauge-Merle; Éric Simoni
      Abstract: Publication date: Available online 8 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Florian Brulfert, Samir Safi, Aurélie Jeanson, Harald Foerstendorf, Stephan Weiss, Catherine Berthomieu, Sandrine Sauge-Merle, Éric Simoni
      The threat of a dirty bomb which could cause internal contamination has been of major concern for the past decades. Because of their high chemical toxicity and their presence in the nuclear fuel cycle, uranium and neptunium are two actinides of high interest. Calmodulin (CaM) which is a ubiquitous protein present in all eukaryotic cells and is involved in calcium-dependent signaling pathways has a known affinity for uranyl and neptunyl ions. The impact of the complexation of these actinides on the physiological response of the protein remains, however, largely unknown. An isothermal titration calorimetry (ITC) was developed to monitor in vitro the enzymatic activity of the phosphodiesterase enzyme which is known to be activated by CaM and calcium. This approach showed that addition of actinyl ions (AnO2 n+), uranyl (UO2 2+) and neptunyl (NpO2 +), resulted in a decrease of the enzymatic activity, due to the formation of CaM-actinide complexes, which inhibit the enzyme and alter its interaction with the substrate by direct interaction. Results from dynamic light scattering rationalized this result by showing that the CaM-actinyl complexes adopted a specific conformation different from that of the CaM-Ca2+ complex. The effect of actinides could be reversed using a hydroxypyridonate actinide decorporation agent (5-LIO(Me-3,2-HOPO)) in the experimental medium demonstrating its capacity to efficiently bind the actinides and restore the calcium-dependent enzyme activation.
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.007
       
  • Cadmium induces Ca2+ mediated, calpain-1/caspase-3-dependent apoptosis in
           primary cultured rat proximal tubular cells
    • Authors: Hong Wang; Nianhui Zhai; Ying Chen; Haibin Xu; Kehe Huang
      Abstract: Publication date: Available online 8 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Hong Wang, Nianhui Zhai, Ying Chen, Haibin Xu, Kehe Huang
      Calcium, as a ubiquitous second messenger, governs a large array of cellular processes and is necessary for cell survival. More recently, it was observed that the cytosolic Ca2+ concentration ([Ca2+]c) elevation could induce apoptosis in primary cultured rat proximal tubular (rPT) cells exposed to cadmium (Cd), but the concrete mechanism is still unclear. This study was designed to investigate the signal pathway involved in [Ca2+]c elevation-mediated apoptosis. The results confirmed the elevation of [Ca2+]c by confocal microscopy and enhancement of the apoptosis by Hoechst 33258 staining and flow cytometer when rPT cells were exposed to Cd for 12h. Then we demonstrated that Cd enhanced the protein levels of active calpain-1 and caspase-3 in rPT cells. Pretreatment with a cytosolic Ca2+ chelator, 1,2-Bis (2-aminophenoxy) ethane-N,N,N′,N′-tetraacetic acid acetoxymethyl ester (BAPTA-AM), markedly blocked the up-regulation of active calpain-1 and caspase-3 and inhibited the apoptosis induced by Cd. Further, rPT cells were pretreated with a cell-permeable selective calpain-1 inhibitor, 3-(4-iodophenyl)-2-mercapto-(Z)-2-propenoic acid (PD150606) and caspase-3 inhibitor, N-Acetyl-Asp-Glu-Val-Asp-CHO (Ac-DEVD-CHO), respectively. PD150606 significantly attenuated the up-regulation of active caspase-3 and the apoptosis induced by Cd. As expected, inhibition of active caspase-3 by Ac-DEVD-CHO decreased the apoptosis induced by Cd. Taken together, it could be concluded that [Ca2+]c elevation did act as a pro-apoptotic signal in Cd-induced cytotoxicity of rPT cells, triggered calpain-1 and caspase-3 activation in turn, and induced apoptosis of rPT cells.
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.005
       
  • New iminodibenzyl derivatives with anti-leishmanial activity
    • Authors: Anderson Arndt; Cleber Wanderlei Liria; Jenicer K.U. Yokoyama-Yasunaka; M. Terêsa Machini; Sílvia Reni Bortolin Uliana; Breno Pannia Espósito
      Abstract: Publication date: Available online 4 April 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Anderson Arndt, Cleber Wanderlei Liria, Jenicer K.U. Yokoyama-Yasunaka, M. Terêsa Machini, Sílvia Reni Bortolin Uliana, Breno Pannia Espósito
      Leishmaniasis is an infection caused by protozoa of the genus Leishmania and transmitted by sandflies. Current treatments are expensive and time-consuming, involving Sb(V)-based compounds, lipossomal amphotericin B and miltefosine. Recent studies suggest that inhibition of trypanothione reductase (TR) could be a specific target in the development of new drugs because it is essential and exclusive to trypanosomatids. This work presents the synthesis and characterization of new iminodibenzyl derivatives (dado) with ethylenediamine (ea), ethanolamine (en) and diethylenetriamine (dien) and their copper(II) complexes. Computational methods indicated that the complexes were highly lipophilic. Pro-oxidant activity assays by oxidation of the dihydrorhodamine (DHR) fluorimetric probe showed that [Cu(dado-ea)]2+ has the highest rate of oxidation, independent of H2O2 concentration. The toxicity to L. amazonensis promastigotes and RAW 264,7 macrophages was assessed, showing that dado-en was the most active new compound. Complexation to copper did not have an appreciable effect on the toxicity of the compounds.
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      PubDate: 2017-04-10T15:05:02Z
      DOI: 10.1016/j.jinorgbio.2017.04.004
       
  • Biochemical characterization of bacterial cytochrome c peroxidase from the
           human pathogen Neisseria gonorrhoeae
    • Authors: Cláudia S. Nóbrega; Mariana Raposo; Gonzalez Van Driessche; Bart Devreese; Sofia R. Pauleta
      Abstract: Publication date: Available online 27 March 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Cláudia S. Nóbrega, Mariana Raposo, Gonzalez Van Driessche, Bart Devreese, Sofia R. Pauleta
      Neisseria gonorrhoeae is an obligate human pathogen that expresses an array of molecular systems to detoxify reactive oxygen species as defense mechanisms during colonization and infection. One of these is the bacterial peroxidase that reduces H2O2 to water in its periplasm. The soluble form of this enzyme was heterologously expressed in E. coli in the holo-form binding two c-types hemes, a high-potential E heme and a low-potential P heme, with redox potentials of (+310mV) and (−190mV/−300mV), respectively in the presence of calcium ions, at pH7.5. Visible and EPR spectroscopic analysis together with activity assays indicates the presence of a calcium dependent reductive activation mechanism in the Neisseria gonorrhoeae bacterial peroxidase, in which P heme is 6cLS bis-His coordinated in the fully oxidized state of the enzyme, and becomes 5cHS upon reduction of E heme in the presence of calcium ions. The activated enzyme has a high affinity for H2O2 (K M of 4±1μM), with maximum activity being attained at pH7.0 and 37°C, with the rate-limiting step in the catalytic cycle being the electron transfer between the two hemes. In this enzyme, dimer formation is not promoted at high ionic strength, thus differing from the classical bacterial peroxidases. These results contribute to the understanding of the involvement of Neisseria gonorrhoeae bacterial peroxidase has a first line defense mechanism against exogenously produced hydrogen peroxide in the host environment.
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      PubDate: 2017-04-03T14:19:41Z
      DOI: 10.1016/j.jinorgbio.2017.03.007
       
  • New tris(dopamine) derivative as an iron chelator. Synthesis, solution
           thermodynamic stability, and antioxidant research
    • Authors: Qingchun Zhang; Bo Jin; Zhaotao Shi; Xiaofang Wang; Shan Lei; Xingyan Tang; Hua Liang; Qiangqiang Liu; Mei Gong; Rufang Peng
      Abstract: Publication date: Available online 21 March 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Qingchun Zhang, Bo Jin, Zhaotao Shi, Xiaofang Wang, Shan Lei, Xingyan Tang, Hua Liang, Qiangqiang Liu, Mei Gong, Rufang Peng
      A new tris(dopamine) derivative, containing three dopamine chelate moieties which were attached to a trimesic acid molecular scaffold, has been prepared and fully characterized by NMR, FTIR and HRMS. The solution thermodynamic stability of the chelator with Fe(III), Mg(II), Zn(II) and Fe(II) ions was investigated. Results demonstrated that the chelator exhibited effective binding ability and improved selectivity to Fe(III) ion. The chelator possessed affinity similar to that of diethylenetriaminepentaacetic acid chelator for Fe(III) ion. The high affinity could be attributed to the favorable geometric arrangement between the chelator and Fe(III) ion coordination preference. The chelator also exhibited high antioxidant activity and nontoxicity to neuron-like rat pheochromocytoma cells. Hence, the chelator could be used as chelating agent for iron overload situations without depleting essential metal ions, such as Mg(II) and Zn(II) ions.
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      PubDate: 2017-03-27T13:49:43Z
      DOI: 10.1016/j.jinorgbio.2017.03.003
       
  • Effect of the protein ligand in DMSO reductase studied by computational
           methods
    • Authors: Geng Dong; Ulf Ryde
      Abstract: Publication date: Available online 21 March 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Geng Dong, Ulf Ryde
      The DMSO reductase family is the largest and most diverse family of mononuclear molybdenum oxygen-atom-transfer proteins. Their active sites contain a Mo ion coordinated to two molybdopterin ligands, one oxo group in the oxidised state, and one additional, often protein-derived ligand. We have used density-functional theory to evaluate how the fourth ligand (serine, cysteine, selenocysteine, OH−, O2−, SH−, or S2−) affects the geometries, reaction mechanism, reaction energies, and reduction potentials of intermediates in the DMSO reductase reaction. Our results show that there are only small changes in the geometries of the reactant and product states, except from the elongation of the MoX bond as the ionic radius of XO, S, Se increases. The five ligands with a single negative charge gave an identical two-step reaction mechanism, in which DMSO first binds to the reduced active site, after which the SO bond is cleaved, concomitantly with the transfer of two electrons from Mo in a rate-determining second transition state. The five models gave similar activation energies of 69–85kJ/mol, with SH− giving the lowest barrier. In contrast, the O2− and S2− ligands gave much higher activation energies (212 and 168kJ/mol) and differing mechanisms (a more symmetric intermediate for O2− and a one-step reaction without any intermediate for S2−). The high activation energies are caused by a less exothermic reaction energy, 13–25kJ/mol, and by a more stable reactant state owing to the strong MoO2− or MoS2− bonds.
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      PubDate: 2017-03-27T13:49:43Z
      DOI: 10.1016/j.jinorgbio.2017.03.004
       
  • Redox behavior and biological properties of ferrocene bearing porphyrins
    • Authors: Rainer Lippert; Tatyana E. Shubina; Sandra Vojnovic; Aleksandar Pavic; Jovana Veselinovic; Jasmina Nikodinovic-Runic; Nada Stankovic; Ivana Ivanović-Burmazović
      Abstract: Publication date: Available online 21 March 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Rainer Lippert, Tatyana E. Shubina, Sandra Vojnovic, Aleksandar Pavic, Jovana Veselinovic, Jasmina Nikodinovic-Runic, Nada Stankovic, Ivana Ivanović-Burmazović
      In order to improve antimicrobial effects of previously studied meso-tetrakis(4-ferrocenylphenyl)porphyrin 1, we have modified its structure by replacing two trans-positioned ferrocenylphenyl moieties with methoxy methylene substituted tert-butylphenyl moieties. Newly synthesized 54,154-bis-(ferrocenyl)-104,204-bis-(tert-butyl)-102,106,202,206-tetrakis-(methoxy-methylene)-5,10,15,20-tetraphenylporphyrin 4 was chemically characterized in detail (by NMR, UV/Vis, IR, MALDI-TOF and ESI MS spectrometry, cyclic voltammetry, prediction of the relative lipophilicity as well as computational methods) and its biological effects were studied in terms of its antibacterial and antifungal activity (both with and without photoactivation), cytotoxicity, hemolysis and DNA cleavage. New ferrocene bearing porphyrin 4 has demonstrated a broader antimicrobial spectrum and modified effects on eukaryotic cells compared to 1. This was discussed in terms of its i) increased lipophilicity, while exhibiting lower toxicity, and ii) the redox potential of a two-electron process that is shifted to lower values, in comparison to ferrocene, thus, entering the physiologically available range and being activated towards redox interactions with biomolecules.
      Graphical abstract image

      PubDate: 2017-03-27T13:49:43Z
      DOI: 10.1016/j.jinorgbio.2017.03.002
       
  • Interaction of a chelating agent,
           5-hydroxy-2-(hydroxymethyl)pyridin-4(1H)-one, with Al(III), Cu(II) and
           Zn(II) ions
    • Authors: Massimiliano Peana; Serenella Medici; Valeria Marina Nurchi; Joanna I. Lachowicz; Guido Crisponi; Eugenio Garribba; Daniele Sanna; Maria Antonietta Zoroddu
      Abstract: Publication date: Available online 16 March 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Massimiliano Peana, Serenella Medici, Valeria Marina Nurchi, Joanna I. Lachowicz, Guido Crisponi, Eugenio Garribba, Daniele Sanna, Maria Antonietta Zoroddu
      5-Hydroxy-2-(hydroxymethyl)pyridin-4(1H)-one ligand, an iron chelator, was evaluated for its coordination ability toward Al(III), Cu(II) and Zn(II) ions by using potentiometric, NMR, EPR and UV–Vis techniques. The behavior of the ligand with the non-essential Al(III) ion has been examined, as well as its potential influence on the homeostatic equilibria of the essential Cu(II) and Zn(II) ions. Structural information on the complex formation equilibria have been obtained from 1D and 2D NMR study. The donor atoms involved in the coordination of Al(III), Cu(II) and Zn(II) ions are (O, O) the same as for Fe(III) at physiological pH value, even if from the complexation competition study the ligand appears to be more selective toward Fe(III) ions supporting that it can be used as an iron chelating agent. The involvement of N-donor atoms at high pH in Cu(II) coordination has been determined by using EPR and UV–Vis techniques.
      Graphical abstract image

      PubDate: 2017-03-20T16:57:09Z
      DOI: 10.1016/j.jinorgbio.2017.03.001
       
  • Interactions of nitrite with catalase: Enzyme activity and reaction
           kinetics studies
    • Authors: Justyna Krych-Madej; Lidia Gebicka
      Abstract: Publication date: Available online 24 February 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Justyna Krych-Madej, Lidia Gebicka
      Catalase, a heme enzyme, which catalyzes decomposition of hydrogen peroxide to water and molecular oxygen, is one of the main enzymes of the antioxidant defense system of the cell. Nitrite, used as a food preservative has long been regarded as a harmful compound due to its ability to form carcinogenic nitrosamines. Recently, much evidence has been presented that nitrite plays a protective role as a nitric oxide donor under hypoxic conditions. In this work the effect of nitrite on the catalytic reactions of catalase was studied. Catalase was inhibited by nitrite, and this process was pH-dependent. IC50 values varied from about 1μM at pH5.0 to about 150μM of nitrite at pH7.4. The presence of chloride significantly enhanced nitrite-induced catalase inhibition, in agreement with earlier observations. The kinetics of the reactions of nitrite with ferric catalase, its redox intermediate, Compound I, and catalase inactive form, Compound II, was also studied. Possible mechanisms of nitrite-induced catalase inhibition are analyzed and the biological consequences of the reactions of catalase with nitrite are discussed.
      Graphical abstract image

      PubDate: 2017-03-01T08:25:56Z
      DOI: 10.1016/j.jinorgbio.2017.02.023
       
  • Inhibition of amyloid peptide fibril formation by gold–sulfur
           complexes
    • Authors: Wenji Wang; Cong Zhao; Dengsen Zhu; Gehui Gong; Weihong Du
      Abstract: Publication date: Available online 21 February 2017
      Source:Journal of Inorganic Biochemistry
      Author(s): Wenji Wang, Cong Zhao, Dengsen Zhu, Gehui Gong, Weihong Du
      Amyloid-related diseases are characterized by protein conformational change and amyloid fibril deposition. Metal complexes are potential inhibitors of amyloidosis. Nitrogen-coordinated gold complexes have been used to disaggregate prion neuropeptide (PrP106-126) and human islet amyloid polypeptide (hIAPP). However, the roles of metal complexes in peptide fibril formation and related bioactivity require further exploration. In this work, we investigated the interactions of amyloid peptides PrP106-126 and hIAPP with two tetracoordinated gold–sulfur complexes, namely, dichloro diethyl dithiocarbamate gold complex and dichloro pyrrolidine dithiocarbamate gold complex. We also determined the effects of these complexes on peptide-induced cytotoxicity. Thioflavin T assay, morphological characterization, and particle size analysis indicated that the two gold–sulfur complexes effectively inhibited the fibrillation of the amyloid peptides, which led to the formation of nanoscale particles. The complexes reduced the cytotoxicity induced by the amyloid peptides. Intrinsic fluorescence, nuclear magnetic resonance, and mass spectrometry revealed that the complexes interacted with PrP106-126 and hIAPP via metal coordination and hydrophobic interaction, which improved the inhibition and binding of the two gold–sulfur compounds. Our study provided new insights into the use of tetracoordinated gold–sulfur complexes as drug candidates against protein conformational disorders.
      Graphical abstract image

      PubDate: 2017-02-21T16:04:25Z
      DOI: 10.1016/j.jinorgbio.2017.02.021
       
 
 
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