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Special Issue "Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioinorganic Chemistry".

Deadline for manuscript submissions: closed (27 March 2016).

Special Issue Editor

Guest Editor
PD. Dr. Eva Freisinger Website E-Mail
Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland
Phone: +41 44 63 546 21
Interests: structures and properties of plant metallothioneins; gene cloning, protein over-expression, and purification; spectroscopic and biochemical characterization of MTs; determination of metal ion binding affinities and redox states; structure determination of MTs by X-ray and NMR

Special Issue Information

Dear Colleagues,

This Special Issue will present a selection of contributions from the 13th International Conference on Applied Bioinorganic Chemistry (ISABC13, http://www.conference.ie/Conferences/index.asp?Conference=384) that was chaired by Prof. Andrea Erxleben at NUI Galway, Ireland, from 12–15 June, 2015. The ISABCs are a biannual conference series organized world-wide. ISABC13 covered a wide range of topics from the field, focused on the central role of metal ions for various biological aspects, such as their interactions with nucleic acids and proteins, their relevance in human disease and application in medicine, their toxicological and environmental roles, and also the application of specific metal ions in bioorganometallic chemistry, such as sensors and as functional compounds of biomaterials.

All speakers presenting a paper at this conference can submit a manuscript for publication. For further information contact the Editorial Office ([email protected]).

PD. Dr. Eva Freisinger
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (9 papers)

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Research

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Open AccessArticle
The X-ray Structures of Six Octameric RNA Duplexes in the Presence of Different Di- and Trivalent Cations
Int. J. Mol. Sci. 2016, 17(7), 988; https://doi.org/10.3390/ijms17070988 - 27 Jun 2016
Cited by 5
Abstract
Due to the polyanionic nature of RNA, the principles of charge neutralization and electrostatic condensation require that cations help to overcome the repulsive forces in order for RNA to adopt a three-dimensional structure. A precise structural knowledge of RNA-metal ion interactions is crucial [...] Read more.
Due to the polyanionic nature of RNA, the principles of charge neutralization and electrostatic condensation require that cations help to overcome the repulsive forces in order for RNA to adopt a three-dimensional structure. A precise structural knowledge of RNA-metal ion interactions is crucial to understand the mechanism of metal ions in the catalytic or regulatory activity of RNA. We solved the crystal structure of an octameric RNA duplex in the presence of the di- and trivalent metal ions Ca2+, Mn2+, Co2+, Cu2+, Sr2+, and Tb3+. The detailed investigation reveals a unique innersphere interaction to uracil and extends the knowledge of the influence of metal ions for conformational changes in RNA structure. Furthermore, we could demonstrate that an accurate localization of the metal ions in the X-ray structures require the consideration of several crystallographic and geometrical parameters as well as the anomalous difference map. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
The Interactions of CPP–ACP with Saliva
Int. J. Mol. Sci. 2016, 17(6), 915; https://doi.org/10.3390/ijms17060915 - 09 Jun 2016
Cited by 1
Abstract
The repair of early dental caries lesions has been demonstrated by the application of the remineralisation technology based on casein phosphopeptide-stabilised amorphous calcium phosphate complexes (CPP–ACP). These complexes consist of an amorphous calcium phosphate mineral phase stabilised and encapsulated by the self-assembly of [...] Read more.
The repair of early dental caries lesions has been demonstrated by the application of the remineralisation technology based on casein phosphopeptide-stabilised amorphous calcium phosphate complexes (CPP–ACP). These complexes consist of an amorphous calcium phosphate mineral phase stabilised and encapsulated by the self-assembly of milk-derived phosphopeptides. During topical application of CPP–ACP complexes in the oral cavity, the CPP encounters the enamel pellicle consisting of salivary proteins and peptides. However the interactions of the CPP with the enamel salivary pellicle are not known. The studies presented here reveal that the predominant peptides of CPP–ACP complexes do interact with specific salivary proteins and peptides of the enamel pellicle, and provide a mechanism by which the CPP–ACP complexes are localised at the tooth surface to promote remineralisation. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
The Effects of Magnesium Ions on the Enzymatic Synthesis of Ligand-Bearing Artificial DNA by Template-Independent Polymerase
Int. J. Mol. Sci. 2016, 17(6), 906; https://doi.org/10.3390/ijms17060906 - 08 Jun 2016
Cited by 8
Abstract
A metal-mediated base pair, composed of two ligand-bearing nucleotides and a bridging metal ion, is one of the most promising components for developing DNA-based functional molecules. We have recently reported an enzymatic method to synthesize hydroxypyridone (H)-type ligand-bearing artificial DNA strands. [...] Read more.
A metal-mediated base pair, composed of two ligand-bearing nucleotides and a bridging metal ion, is one of the most promising components for developing DNA-based functional molecules. We have recently reported an enzymatic method to synthesize hydroxypyridone (H)-type ligand-bearing artificial DNA strands. Terminal deoxynucleotidyl transferase (TdT), a template-independent DNA polymerase, was found to oligomerize H nucleotides to afford ligand-bearing DNAs, which were subsequently hybridized through copper-mediated base pairing (H–CuIIH). In this study, we investigated the effects of a metal cofactor, MgII ion, on the TdT-catalyzed polymerization of H nucleotides. At a high MgII concentration (10 mM), the reaction was halted after several H nucleotides were appended. In contrast, at lower MgII concentrations, H nucleotides were further appended to the H-tailed product to afford longer ligand-bearing DNA strands. An electrophoresis mobility shift assay revealed that the binding affinity of TdT to the H-tailed DNAs depends on the MgII concentration. In the presence of excess MgII ions, TdT did not bind to the H-tailed strands; thus, further elongation was impeded. This is possibly because the interaction with MgII ions caused folding of the H-tailed strands into unfavorable secondary structures. This finding provides an insight into the enzymatic synthesis of longer ligand-bearing DNA strands. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
6-Pyrazolylpurine as an Artificial Nucleobase for Metal-Mediated Base Pairing in DNA Duplexes
Int. J. Mol. Sci. 2016, 17(4), 554; https://doi.org/10.3390/ijms17040554 - 14 Apr 2016
Cited by 5
Abstract
The artificial nucleobase 6-pyrazol-1-yl-purine (6PP) has been investigated with respect to its usability in metal-mediated base pairing. As was shown by temperature-dependent UV spectroscopy, 6PP may form weakly stabilizing 6PP–Ag(I)–6PP homo base pairs. Interestingly, 6PP can be used to selectively recognize a complementary [...] Read more.
The artificial nucleobase 6-pyrazol-1-yl-purine (6PP) has been investigated with respect to its usability in metal-mediated base pairing. As was shown by temperature-dependent UV spectroscopy, 6PP may form weakly stabilizing 6PP–Ag(I)–6PP homo base pairs. Interestingly, 6PP can be used to selectively recognize a complementary pyrimidine nucleobase. The addition of Ag(I) to a DNA duplex comprising a central 6PP:C mispair (C = cytosine) leads to a slight destabilization of the duplex. In contrast, a stabilizing 6PP–Ag(I)–T base pair is formed with a complementary thymine (T) residue. It is interesting to note that 6PP is capable of differentiating between the pyrimidine moieties despite the fact that it is not as sterically crowded as 6-(3,5-dimethylpyrazol-1-yl)purine, an artificial nucleobase that had previously been suggested for the recognition of nucleic acid sequences via the formation of a metal-mediated base pair. Hence, the additional methyl groups of 6-(3,5-dimethylpyrazol-1-yl)purine may not be required for the specific recognition of the complementary nucleobase. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
Localization and Spectroscopic Analysis of the Cu(I) Binding Site in Wheat Metallothionein Ec-1
Int. J. Mol. Sci. 2016, 17(3), 371; https://doi.org/10.3390/ijms17030371 - 11 Mar 2016
Cited by 4
Abstract
The early cysteine-labeled metallothionein (MT) from Triticum aestivum (common wheat), denoted Ec-1, features two structurally well-defined domains, γ and βE, coordinating two and four Zn(II) ions, respectively. While the protein is currently assumed to function mainly in zinc homeostasis, [...] Read more.
The early cysteine-labeled metallothionein (MT) from Triticum aestivum (common wheat), denoted Ec-1, features two structurally well-defined domains, γ and βE, coordinating two and four Zn(II) ions, respectively. While the protein is currently assumed to function mainly in zinc homeostasis, a low amount of copper ions was also recently detected in a native Ec-1 sample. To evaluate the observed copper binding in more detail, the recombinant Zn6Ec-1 form was exposed to different amounts of Cu(I) ions and the resulting species characterized with spectroscopic methods. Data reveal that the first Cu(I) equivalent coordinates exclusively to the N-terminal γ-domain of the protein and replaces one Zn(II) ion. To analyze the ability of the γ-domain for coordination of monovalent metal ions in more detail, the γ-Ec-1 peptide fragment was incubated with increasing amounts of Cu(I) and the process monitored with UV–VIS, circular dichroism, and luminescence spectroscopy. Closely similar spectra are observed regardless if the apo- or the metal ion-loaded and, hence, pre-folded forms, were used for the titration experiments with Cu(I). The results indicate that low amounts of Cu(I) ions displace the two metal ions subsequently and stoichiometrically, despite the different coordination geometry requirements of Cu(I) and Zn(II). Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
Ruthenium(III) Complexes of Heterocyclic Tridentate (ONN) Schiff Base: Synthesis, Characterization and its Biological Properties as an Antiradical and Antiproliferative Agent
Int. J. Mol. Sci. 2016, 17(1), 60; https://doi.org/10.3390/ijms17010060 - 04 Jan 2016
Cited by 9
Abstract
The current work reports the synthesis, spectroscopic studies, antiradical and antiproliferative properties of four ruthenium(III) complexes of heterocyclic tridentate Schiff base bearing a simple 2′,4′-dihydroxyacetophenone functionality and ethylenediamine as the bridging ligand with RCHO moiety. The reaction of the tridentate ligands with RuCl [...] Read more.
The current work reports the synthesis, spectroscopic studies, antiradical and antiproliferative properties of four ruthenium(III) complexes of heterocyclic tridentate Schiff base bearing a simple 2′,4′-dihydroxyacetophenone functionality and ethylenediamine as the bridging ligand with RCHO moiety. The reaction of the tridentate ligands with RuCl3·3H2O lead to the formation of neutral complexes of the type [Ru(L)Cl2(H2O)] (where L = tridentate NNO ligands). The compounds were characterized by elemental analysis, UV-vis, conductivity measurements, FTIR spectroscopy and confirmed the proposed octahedral geometry around the Ru ion. The Ru(III) compounds showed antiradical potentials against 2,2-Diphenyl-1-Picrylhydrazyl (DPPH) and 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radicals, with DPPH scavenging capability in the order: [(PAEBOD)RuCl2] > [(BZEBOD)RuCl2] > [(MOABOD)RuCl2] > [Vit. C] > [rutin] > [(METBOD)RuCl2], and ABTS radical in the order: [(PAEBOD)RuCl2] < [(MOABOD)RuCl2] < [(BZEBOD)RuCl2] < [(METBOD)RuCl2]. Furthermore, in vitro anti-proliferative activity was investigated against three human cancer cell lines: renal cancer cell (TK-10), melanoma cancer cell (UACC-62) and breast cancer cell (MCF-7) by SRB assay. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
Identification of Arsenic Direct-Binding Proteins in Acute Promyelocytic Leukaemia Cells
Int. J. Mol. Sci. 2015, 16(11), 26871-26879; https://doi.org/10.3390/ijms161125994 - 10 Nov 2015
Cited by 3
Abstract
The identification of arsenic direct-binding proteins is essential for determining the mechanism by which arsenic trioxide achieves its chemotherapeutic effects. At least two cysteines close together in the amino acid sequence are crucial to the binding of arsenic and essential to the identification [...] Read more.
The identification of arsenic direct-binding proteins is essential for determining the mechanism by which arsenic trioxide achieves its chemotherapeutic effects. At least two cysteines close together in the amino acid sequence are crucial to the binding of arsenic and essential to the identification of arsenic-binding proteins. In the present study, arsenic binding proteins were pulled down with streptavidin and identified using a liquid chromatograph-mass spectrometer (LC-MS/MS). More than 40 arsenic-binding proteins were separated, and redox-related proteins, glutathione S-transferase P1 (GSTP1), heat shock 70 kDa protein 9 (HSPA9) and pyruvate kinase M2 (PKM2), were further studied using binding assays in vitro. Notably, PKM2 has a high affinity for arsenic. In contrast to PKM2, GSTP1and HSPA9 did not combine with arsenic directly in vitro. These observations suggest that arsenic-mediated acute promyelocytic leukaemia (APL) suppressive effects involve PKM2. In summary, we identified several arsenic binding proteins in APL cells and investigated the therapeutic mechanisms of arsenic trioxide for APL. Further investigation into specific signal pathways by which PKM2 mediates APL developments may lead to a better understanding of arsenic effects on APL. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Open AccessArticle
Structural Diversity of Copper(II) Complexes with 9-Deazahypoxanthine and Their in Vitro SOD-Like Activity
Int. J. Mol. Sci. 2015, 16(7), 15954-15970; https://doi.org/10.3390/ijms160715954 - 14 Jul 2015
Cited by 3
Abstract
Two structurally different copper(II) complexes of the compositions [{Cu(9dhx)(H2O)3}2(µ-SO4)2] (1) and [Cu(9dhx)2(H2O)2(NO3)2]·H2O (2), involving 9-deazahypoxanthine (9dhx; 6-oxo-9-deazapurine; [...] Read more.
Two structurally different copper(II) complexes of the compositions [{Cu(9dhx)(H2O)3}2(µ-SO4)2] (1) and [Cu(9dhx)2(H2O)2(NO3)2]·H2O (2), involving 9-deazahypoxanthine (9dhx; 6-oxo-9-deazapurine; 9-deazahypoxanthine), have been prepared and characterized by elemental analysis, infrared and electronic spectroscopy, electrospray ionisation (ESI) mass spectrometry, thermogravimetric (TG) and differential thermal (DTA) analyses, and cyclic voltammetry. The X-ray structures of complexes 1 and [Cu(9dhx)2(H2O)2(NO3)2] (2a) revealed the distorted octahedral geometry in the vicinity of the copper(II) atoms, with the NO5 and N2O4 donor set, respectively. In the dimeric compound 1, the {Cu(9dhx)(H2O)3}2 units are bridged by sulfate groups with the Cu···Cu separation being 5.3446(2) Å. In both structures the 9dhx ligands are coordinated through the N3 atoms of the pyrimidine moieties. The SOD-like activity of complexes 1 and 2 was evaluated in vitro showing moderate effect, with the IC50 values equal to 18.20, and 53.33 μM, respectively. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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Review

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Open AccessReview
Vanadium Compounds as Pro-Inflammatory Agents: Effects on Cyclooxygenases
Int. J. Mol. Sci. 2015, 16(6), 12648-12668; https://doi.org/10.3390/ijms160612648 - 04 Jun 2015
Cited by 14
Abstract
This paper discusses how the activity and expression of cyclooxygenases are influenced by vanadium compounds at anticancer concentrations and recorded in inorganic vanadium poisonings. We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on [...] Read more.
This paper discusses how the activity and expression of cyclooxygenases are influenced by vanadium compounds at anticancer concentrations and recorded in inorganic vanadium poisonings. We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on their impact on intracellular signaling. We describe the exact mechanism of the effect of vanadium compounds on protein tyrosine phosphatases (PTP), epidermal growth factor receptor (EGFR), PLCγ, Src, mitogen-activated protein kinase (MAPK) cascades, transcription factor NF-κB, the effect on the proteolysis of COX-2 and the activity of cPLA2. For a better understanding of these processes, a lot of space is devoted to the transformation of vanadium compounds within the cell and the molecular influence on the direct targets of the discussed vanadium compounds. Full article
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
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