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Inorganics
Special Issues
Metal Complexes with Biological Functions
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Metal Complexes with Biological Functions

A special issue of Inorganics (ISSN 2304-6740). This special issue belongs to the section "Bioinorganic Chemistry".

Deadline for manuscript submissions: closed (31 July 2020) | Viewed by 13759

Special Issue Editor

Prof. Dr. Nora Kulak

E-Mail Website
Guest Editor
Institute of Chemistry, Otto-von-Guericke-Universität Magdeburg, Universitätsplatz 2, 39106 Magdeburg, Germany
Interests: metal-based artificial nucleases, proteases and enzyme inhibitors; metallopeptides; fluorinated ligand systems; supramolecular aggregation and immobilization of metal complexes

Special Issue Information

Dear Colleagues,

Metal ions play a vital role in biological processes like signal transduction, electron transport, and promoting or inhibiting biomolecule synthesis, and as active centers in metalloenzymes. Metal complexes synthesized in the lab can be designed for mimicking such metal-based functions inside or outside cells. Usually, the redox activity and/or Lewis acidity of transition metal ions allow for such behavior, but also ligands can render a metal complex biologically active. The interactions of metal complexes with biomolecules and cellular components can result in cytotoxic and antimicrobial properties.

The Special Issue “Metal Complexes with Biological Functions” covers new developments in the design of metal complexes regarding their interactions with biomolecules (e.g., artificial nucleases and proteases), regarding enzyme mimicry, and regarding medicinal purposes based on their action as cytotoxic and antimicrobial agents.

Prof. Dr. Nora Kulak
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 submissions that pass pre-check are 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. Inorganics 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 2700 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

  • nucleic acids
  • proteins
  • metalloenzymes
  • artificial enzymes
  • artificial nucleases
  • artificial proteases
  • cytotoxicity
  • antimicrobials

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Published Papers (2 papers)

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Research

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23 pages, 23280 KiB  
Article
Copper(II) Complexes with Tetradentate Piperazine-Based Ligands: DNA Cleavage and Cytotoxicity
by Sebastian Doniz Kettenmann, Yvonne Nossol, Febee R. Louka, Julia R. Legrande, Elise Marine, Roland C. Fischer, Franz A. Mautner, Vinja Hergl, Nora Kulak and Salah S. Massoud
Inorganics 2021, 9(2), 12; https://doi.org/10.3390/inorganics9020012 - 1 Feb 2021
Cited by 19 | Viewed by 4210
Abstract
Five-coordinate Cu(II) complexes, [Cu(Ln)X]ClO4/PF6, where Ln = piperazine ligands bearing two pyridyl arms and X = ClO4− for Ln = L1 (1-ClO4), L2 (2-ClO4), L [...] Read more.
Five-coordinate Cu(II) complexes, [Cu(Ln)X]ClO4/PF6, where Ln = piperazine ligands bearing two pyridyl arms and X = ClO4− for Ln = L1 (1-ClO4), L2 (2-ClO4), L3 (3-ClO4), and L6 (6-ClO4) as well as [Cu(Ln)Cl]PF6 for Ln = L1 (1-Cl), L4 (4-Cl), and L5 (5-Cl) have been synthesized and characterized by spectroscopic techniques. The molecular structures of the last two complexes were determined by X-ray crystallography. In aqueous acetonitrile solutions, molar conductivity measurements and UV-VIS spectrophotometric titrations of the complexes revealed the hydrolysis of the complexes to [Cu(Ln)(H2O)]2+ species. The biological activity of the Cu(II) complexes with respect to DNA cleavage and cytotoxicity was investigated. At micromolar concentration within 2 h and pH 7.4, DNA cleavage rate decreased in the order: 1-Cl ≈ 1-ClO4 > 3-ClO4 ≥ 2-ClO4 with cleavage enhancements of up to 23 million. Complexes 4-Cl, 5-Cl, and 6-ClO4 were inactive. In order to elucidate the cleavage mechanism, the cleavage of bis(4-nitrophenyl)phosphate (BNPP) and reactive oxygen species (ROS) quenching studies were conducted. The mechanistic pathway of DNA cleavage depends on the ligand’s skeleton: while an oxidative pathway was preferable for 1-Cl/1-ClO4, DNA cleavage by 2-ClO4 and 3-ClO4 predominantly proceeds via a hydrolytic mechanism. Complexes 1-ClO4, 3-ClO4, and 5-Cl were found to be cytotoxic against A2780 cells (IC50 30–40 µM). In fibroblasts, the IC50 value was much higher for 3-ClO4 with no toxic effect. Full article
(This article belongs to the Special Issue Metal Complexes with Biological Functions)
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Review

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35 pages, 9152 KiB  
Review
Exploring Serum Transferrin Regulation of Nonferric Metal Therapeutic Function and Toxicity
by Josué A. Benjamín-Rivera, Andrés E. Cardona-Rivera, Ángel L. Vázquez-Maldonado, Christian Y. Dones-Lassalle, Héctor L. Pabón-Colon, Héctor M. Rodríguez-Rivera, Israel Rodríguez, Jean C. González-Espiet, Jessika Pazol, Jobaniel D. Pérez-Ríos, José F. Catala-Torres, Marielie Carrasquillo Rivera, Michael G. De Jesus-Soto, Nicolle A. Cordero-Virella, Paola M. Cruz-Maldonado, Patricia González-Pagan, Raul Hernández-Ríos, Kavita Gaur, Sergio A. Loza-Rosas and Arthur D. Tinoco
Inorganics 2020, 8(9), 48; https://doi.org/10.3390/inorganics8090048 - 29 Aug 2020
Cited by 22 | Viewed by 8865
Abstract
Serum transferrin (sTf) plays a pivotal role in regulating iron biodistribution and homeostasis within the body. The molecular details of sTf Fe(III) binding blood transport, and cellular delivery through transferrin receptor-mediated endocytosis are generally well-understood. Emerging interest exists in exploring sTf complexation of [...] Read more.
Serum transferrin (sTf) plays a pivotal role in regulating iron biodistribution and homeostasis within the body. The molecular details of sTf Fe(III) binding blood transport, and cellular delivery through transferrin receptor-mediated endocytosis are generally well-understood. Emerging interest exists in exploring sTf complexation of nonferric metals as it facilitates the therapeutic potential and toxicity of several of them. This review explores recent X-ray structural and physiologically relevant metal speciation studies to understand how sTf partakes in the bioactivity of key non-redox active hard Lewis acidic metals. It challenges preconceived notions of sTf structure function correlations that were based exclusively on the Fe(III) model by revealing distinct coordination modalities that nonferric metal ions can adopt and different modes of binding to metal-free and Fe(III)-bound sTf that can directly influence how they enter into cells and, ultimately, how they may impact human health. This knowledge informs on biomedical strategies to engineer sTf as a delivery vehicle for metal-based diagnostic and therapeutic agents in the cancer field. It is the intention of this work to open new avenues for characterizing the functionality and medical utility of nonferric-bound sTf and to expand the significance of this protein in the context of bioinorganic chemistry. Full article
(This article belongs to the Special Issue Metal Complexes with Biological Functions)
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