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Special Issue "Metallopeptides"

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".

Deadline for manuscript submissions: closed (20 June 2017)

Special Issue Editor

Guest Editor
Prof. Dr. Miguel Vázquez López

Departamento de Química Inorgánica y Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CIQUS), Universidade de Santiago de Compostela, 15782 Santiago de Compostela, Spain
Website | E-Mail
Interests: supramolecular chemistry; chemical biology; coordination chemistry; self-assembly; biosensing; biolabeling; molecular devices and machines; DNA-binding; theranostic drugs; peptides and metallopeptides; helicates

Special Issue Information

Dear Colleagues,

Metalloproteins can be defined as those proteins that contain at least one metal ion in their structure. Diverse studies estimate that about one third of all proteins need of metal ions to correctly perform their functions, including catalysis, transport, signal transduction, storage, detoxification or DNA transcription, among others. Over the last thirty years, many groups have focused their research efforts in understand the structural, folding and functional aspects of metalloproteins, and applying this knowledge to the design of new systems with novel and improved structural, spectroscopic, biological or catalytic properties. However, the large size of most metalloproteins requires their production by in vitro expression, so that the introduction of extrinsic functionalities typically requires cumbersome protocols, or postsynthetic modifications, which typically suffer from poor selectivity.

On the other hand, metallopeptides encode in their amino acid sequence precise structural and functional information, and represent excellent model systems that can be used as simplified mimetics of metalloproteins. In contrast with them, metallopeptides can be easily synthesized, modified and functionalized through chemical means, and can be easily and quickly produced in large quantities. Therefore, the scientific interest of the synthetic, structural and folding aspects of metallopeptides, as well as their functional application in a variety of areas has exponentially increased in the last few years.

Furthermore, the metallopeptides are not limited to systems built with the set of twenty natural amino acids, and allow the straightforward incorporation in their sequence of unnatural coordinating amino acids equipped with chelating ligands, such as 2,2′-bipyridine or 2,2′:6′,2′′-terpyridine, which greatly simplify the creation of appropriate coordinating environments and the definition of the microarchitecture of the peptide ligands to create artificial metal-peptide hybrids that potentially combine the functional versatility of metal complexes with the biological properties of peptide systems.

This Special Issue of Molecules wants to highlight this multidisciplinary scientific subject of increasing interest and enormous potential. Original research, as well as review papers dealing with all aspects of natural and unnatural metallopeptides, including synthesis, structural and folding properties and functional applications in catalysis, metal storage, metal transport, metal detoxification, DNA-binding, biosensing, biolabeling, etc., or as antibacterial/cytotoxic drugs, molecular machines, etc., are welcome for inclusion in this Special Issue of Molecules.

Prof. Miguel Vázquez López
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.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). 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.

Keywords

  • metallopeptide synthesis
  • structural aspects
  • folding of metallopeptides
  • DNA-binding
  • catalysis
  • biosensing
  • bioconjugation
  • molecular machines
  • metal detoxification
  • transport and storage
  • theranostic drugs
  • ionophores
  • chemical biology
  • supramolecular chemistry
  • medicinal chemistry and biomaterials

Published Papers (6 papers)

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Research

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Open AccessArticle The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions
Molecules 2017, 22(11), 1904; doi:10.3390/molecules22111904
Received: 13 October 2017 / Revised: 29 October 2017 / Accepted: 2 November 2017 / Published: 5 November 2017
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Abstract
The Dps protein of Escherichia coli, which combines ferroxidase activity and the ability to bind DNA, is effectively used by bacteria to protect their genomes from damage. Both activities depend on the integrity of this multi-subunit protein, which has an inner cavity
[...] Read more.
The Dps protein of Escherichia coli, which combines ferroxidase activity and the ability to bind DNA, is effectively used by bacteria to protect their genomes from damage. Both activities depend on the integrity of this multi-subunit protein, which has an inner cavity for iron oxides; however, the diversity of its oligomeric forms has only been studied fragmentarily. Here, we show that iron ions stabilize the dodecameric form of Dps. This was found by electrophoretic fractionation and size exclusion chromatography, which revealed several oligomers in highly purified protein samples and demonstrated their conversion to dodecamers in the presence of 1 mM Mohr’s salt. The transmission electron microscopy data contradicted the assumption that the stabilizing effect is given by the optimal core size formed in the inner cavity of Dps. The charge state of iron ions was evaluated using Mössbauer spectroscopy, which showed the presence of Fe3O4, rather than the expected Fe2O3, in the sample. Assuming that Fe2+ can form additional inter-subunit contacts, we modeled the interaction of FeO and Fe2O3 with Dps, but the binding sites with putative functionality were predicted only for Fe2O3. The question of how the dodecameric form can be stabilized by ferric oxides is discussed. Full article
(This article belongs to the Special Issue Metallopeptides)
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Open AccessArticle Structure and Catalysis of Fe(III) and Cu(II) Microperoxidase-11 Interacting with the Positively Charged Interfaces of Lipids
Molecules 2017, 22(8), 1212; doi:10.3390/molecules22081212
Received: 6 May 2017 / Revised: 20 June 2017 / Accepted: 14 July 2017 / Published: 26 July 2017
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Abstract
Numerous applications have been described for microperoxidases (MPs) such as in photoreceptors, sensing, drugs, and hydrogen evolution. The last application was obtained by replacing Fe(III), the native central metal, by cobalt ion and inspired part of the present study. Here, the Fe(III) of
[...] Read more.
Numerous applications have been described for microperoxidases (MPs) such as in photoreceptors, sensing, drugs, and hydrogen evolution. The last application was obtained by replacing Fe(III), the native central metal, by cobalt ion and inspired part of the present study. Here, the Fe(III) of MP-11 was replaced by Cu(II) that is also a stable redox state in aerated medium, and the structure and activity of both MPs were modulated by the interaction with the positively charged interfaces of lipids. Comparative spectroscopic characterization of Fe(III) and Cu(II)MP-11 in the studied media demonstrated the presence of high and low spin species with axial distortion. The association of the Fe(III)MP-11 with CTAB and Cu(II)MP-11 with DODAB affected the colloidal stability of the surfactants that was recovered by heating. This result is consistent with hydrophobic interactions of MPs with DODAB vesicles and CTAB micelles. The hydrophobic interactions decreased the heme accessibility to substrates and the Fe(III) MP-11catalytic efficiency. Cu(II)MP-11 challenged by peroxides exhibited a cyclic Cu(II)/Cu(I) interconversion mechanism that is suggestive of a mimetic Cu/ZnSOD (superoxide dismutase) activity against peroxides. Hydrogen peroxide-activated Cu(II)MP-11 converted Amplex Red® to dihydroresofurin. This study opens more possibilities for technological applications of MPs. Full article
(This article belongs to the Special Issue Metallopeptides)
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Open AccessArticle Advantages of an Electrochemical Method Compared to the Spectrophotometric Kinetic Study of Peroxidase Inhibition by Boroxine Derivative
Molecules 2017, 22(7), 1120; doi:10.3390/molecules22071120
Received: 29 May 2017 / Accepted: 3 July 2017 / Published: 5 July 2017
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Abstract
In this study, boroxine derivative (K2[B3O3F4OH]) was tested as an inhibitor of horseradish peroxidase (HRP) by spectrophotometric and electrochemical methods. The activity of horseradish peroxidase was first studied under steady-state kinetic conditions by a spectrophotometric
[...] Read more.
In this study, boroxine derivative (K2[B3O3F4OH]) was tested as an inhibitor of horseradish peroxidase (HRP) by spectrophotometric and electrochemical methods. The activity of horseradish peroxidase was first studied under steady-state kinetic conditions by a spectrophotometric method which required the use of guaiacol as a second substrate to measure guaiacol peroxidation. The results of this method have shown that, by changing the concentration of guaiacol as the literature suggests, a different type of inhibition is observed than when changing the concentration of hydrogen peroxide as the substrate. This suggests that guaiacol interferes with the reaction in some way. The electrochemical method involves direct electron transfer of HRP immobilized in Nafion nanocomposite films on a glassy carbon (GC) electrode, creating a sensor with an electro-catalytic response to the reduction of hydrogen peroxide. The electrochemical method simplifies kinetic assays by removing the requirement of reducing substrates. Full article
(This article belongs to the Special Issue Metallopeptides)
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Open AccessArticle Mechanistic Explanation of the Weak Carbonic Anhydrase’s Esterase Activity
Molecules 2017, 22(6), 1009; doi:10.3390/molecules22061009
Received: 10 May 2017 / Revised: 8 June 2017 / Accepted: 13 June 2017 / Published: 18 June 2017
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Abstract
In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA’s inhibitor is of potential relevance in cancer therapy.
[...] Read more.
In order to elucidate the elementary mechanism of the promiscuous esterase activity of human carbonic anhydrase (h-CA), we present an accurate theoretical investigation on the hydrolysis of fully-acetylated d-glucose functionalized as sulfamate. This h-CA’s inhibitor is of potential relevance in cancer therapy. The study has been performed within the framework of three-layer ONIOM (QM-high:QM’-medium:MM-low) hybrid approach. The computations revealed that the hydrolysis process is not energetically favored, in agreement with the observed weak carbonic anhydrase’s esterase activity. Full article
(This article belongs to the Special Issue Metallopeptides)
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Review

Jump to: Research

Open AccessReview Understanding of MYB Transcription Factors Involved in Glucosinolate Biosynthesis in Brassicaceae
Molecules 2017, 22(9), 1549; doi:10.3390/molecules22091549
Received: 12 August 2017 / Revised: 8 September 2017 / Accepted: 12 September 2017 / Published: 14 September 2017
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Abstract
Glucosinolates (GSLs) are widely known secondary metabolites that have anticarcinogenic and antioxidative activities in humans and defense roles in plants of the Brassicaceae family. Some R2R3-type MYB (myeloblastosis) transcription factors (TFs) control GSL biosynthesis in Arabidopsis. However, studies on the MYB TFs
[...] Read more.
Glucosinolates (GSLs) are widely known secondary metabolites that have anticarcinogenic and antioxidative activities in humans and defense roles in plants of the Brassicaceae family. Some R2R3-type MYB (myeloblastosis) transcription factors (TFs) control GSL biosynthesis in Arabidopsis. However, studies on the MYB TFs involved in GSL biosynthesis in Brassica species are limited because of the complexity of the genome, which includes an increased number of paralog genes as a result of genome duplication. The recent completion of the genome sequencing of the Brassica species permits the identification of MYB TFs involved in GSL biosynthesis by comparative genome analysis with A. thaliana. In this review, we describe various findings on the regulation of GSL biosynthesis in Brassicaceae. Furthermore, we identify 63 orthologous copies corresponding to five MYB TFs from Arabidopsis, except MYB76 in Brassica species. Fifty-five MYB TFs from the Brassica species possess a conserved amino acid sequence in their R2R3 MYB DNA-binding domain, and share close evolutionary relationships. Our analysis will provide useful information on the 55 MYB TFs involved in the regulation of GSL biosynthesis in Brassica species, which have a polyploid genome. Full article
(This article belongs to the Special Issue Metallopeptides)
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Open AccessReview The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase
Molecules 2017, 22(9), 1429; doi:10.3390/molecules22091429
Received: 19 July 2017 / Revised: 22 August 2017 / Accepted: 27 August 2017 / Published: 29 August 2017
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Abstract
Protein misfolding and conformational changes are common hallmarks in many neurodegenerative diseases involving formation and deposition of toxic protein aggregates. Although many players are involved in the in vivo protein aggregation, physiological factors such as labile metal ions within the cellular environment are
[...] Read more.
Protein misfolding and conformational changes are common hallmarks in many neurodegenerative diseases involving formation and deposition of toxic protein aggregates. Although many players are involved in the in vivo protein aggregation, physiological factors such as labile metal ions within the cellular environment are likely to play a key role. In this review, we elucidate the role of metal binding in the aggregation process of copper-zinc superoxide dismutase (SOD1) associated to amyotrophic lateral sclerosis (ALS). SOD1 is an extremely stable Cu-Zn metalloprotein in which metal binding is crucial for folding, enzymatic activity and maintenance of the native conformation. Indeed, demetalation in SOD1 is known to induce misfolding and aggregation in physiological conditions in vitro suggesting that metal binding could play a key role in the pathological aggregation of SOD1. In addition, this study includes recent advances on the role of aberrant metal coordination in promoting SOD1 aggregation, highlighting the influence of metal ion homeostasis in pathologic aggregation processes. Full article
(This article belongs to the Special Issue Metallopeptides)
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