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Special Issue "Metallodrugs: Mechanisms of Action, Molecular Targets and Biological Activity"

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

Deadline for manuscript submissions: 30 June 2021.

Special Issue Editors

Prof. Dr. Antonello Merlino
Website
Guest Editor
Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo, Via Cintia, Napoli, Italy
Interests: protein-metal based drug adducts; X-Ray crystallography; protein metalation; protein-ligand interactions
Special Issues and Collections in MDPI journals
Dr. Giarita Ferraro
Website
Guest Editor
Department of Chemistry “Ugo Schiff”, University of Florence, Sesto Fiorentino, Italy

Special Issue Information

Since the serendipitous discovery of the cytotoxic activity of cisplatin at the end of the 1960s, Pt- and non-Pt-based compounds have been extensively studied as potential anticancer agents. Metal compounds also play an important role in clinics as antimicrobial, antiviral or antiarthritic agents. A deep knowledge of their mode of action and of their biological targets may help in the design of new molecules with improved biological activities and limited side effects.

This Special Issue of International Journal of Molecular Science on “Metallodrugs: mechanisms of action, molecular targets and biological activity” aims to collect original contributions, letters or review articles describing recent advances in this field.

Topics include, but are not limited to, the synthesis and characterization, including structures and applications, of novel metal compounds with biological activities, insights into stability and reactivity of these compounds, insights into the mechanism of action, potential targets, and biological activity of metallodrugs. The Issue will also collect articles describing the interaction of metallodrugs with biological macromolecules, based on experimental techniques (NMR, X-ray crystallography, mass spectrometry etc.) or using computational approaches.

Prof. Dr. Antonello Merlino
Dr. Giarita Ferraro
Guest Editors

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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.

Keywords

  • Metal-based drugs
  • Protein metalation
  • Coordination chemistry
  • Metal binding sites
  • Organometallic compounds

Published Papers (2 papers)

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Research

Open AccessArticle
Arsenoplatin-Ferritin Nanocage: Structure and Cytotoxicity
Int. J. Mol. Sci. 2021, 22(4), 1874; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22041874 - 13 Feb 2021
Abstract
Arsenoplatin-1 (AP-1), the prototype of a novel class of metallodrugs containing a PtAs(OH)2 core, was encapsulated within the apoferritin (AFt) nanocage. UV-Vis absorption spectroscopy and inductively coupled plasma-atomic emission spectroscopy measurements confirmed metallodrug encapsulation and allowed us to determine the average amount [...] Read more.
Arsenoplatin-1 (AP-1), the prototype of a novel class of metallodrugs containing a PtAs(OH)2 core, was encapsulated within the apoferritin (AFt) nanocage. UV-Vis absorption spectroscopy and inductively coupled plasma-atomic emission spectroscopy measurements confirmed metallodrug encapsulation and allowed us to determine the average amount of AP-1 trapped inside the cage. The X-ray structure of AP-1-encapsulated AFt was solved at 1.50 Å. Diffraction data revealed that an AP-1 fragment coordinates the side chain of a His residue. The biological activity of AP-1-loaded AFt was comparatively tested on a few representative cancer and non-cancer cell lines. Even though the presence of the cage reduces the overall cytotoxicity of AP-1, it improves its selectivity towards cancer cells. Full article
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Open AccessArticle
Unusual Structural Features in the Adduct of Dirhodium Tetraacetate with Lysozyme
Int. J. Mol. Sci. 2021, 22(3), 1496; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22031496 - 02 Feb 2021
Abstract
The structures of the adducts formed upon reaction of the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] with the model protein hen egg white lysozyme (HEWL) under different experimental conditions are reported. Results indicate that [Rh2 [...] Read more.
The structures of the adducts formed upon reaction of the cytotoxic paddlewheel dirhodium complex [Rh2(μ-O2CCH3)4] with the model protein hen egg white lysozyme (HEWL) under different experimental conditions are reported. Results indicate that [Rh2(μ-O2CCH3)4] extensively reacts with HEWL:it in part breaks down, at variance with what happens in reactions with other proteins. A Rh center coordinates the side chains of Arg14 and His15. Dimeric Rh–Rh units with Rh–Rh distances between 2.3 and 2.5 Å are bound to the side chains of Asp18, Asp101, Asn93, and Lys96, while a dirhodium unit with a Rh–Rh distance of 3.2–3.4 Å binds the C-terminal carboxylate and the side chain of Lys13 at the interface between two symmetry-related molecules. An additional monometallic fragment binds the side chain of Lys33. These data, which are supported by replicated structural determinations, shed light on the reactivity of dirhodium tetracarboxylates with proteins, providing useful information for the design of new Rh-containing biomaterials with an array of potential applications in the field of catalysis or of medicinal chemistry and valuable insight into the mechanism of action of these potential anticancer agents. Full article
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