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Peptide and Protein Metalation
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Peptide and Protein Metalation

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

Deadline for manuscript submissions: 20 March 2026 | Viewed by 601

Special Issue Editors

Prof. Dr. Antonello Merlino

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Guest Editor
Department of Chemical Sciences, University of Naples Federico II (Complesso Universitario di Monte Sant'Angelo), Via Cintia, 80126 Napoli, Italy
Interests: protein crystallography; protein metalation; metallodrugs; protein–metal-based drug adducts; X-ray crystallography; protein–ligand interactions
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Irene Russo Krauss

E-Mail Website
Guest Editor
Department of Chemical Sciences, University of Naples Federico II (Complesso Universitario di Monte Sant’Angelo), Via Cintia, 80126 Napoli, Italy
Interests: protein structure; protein interactions; protein–nanoparticle interaction; scattering; spectroscopy
Special Issues, Collections and Topics in MDPI journals
Dr. Giarita Ferraro

E-Mail Website
Guest Editor
Department of Chemical Sciences, University of Naples Federico II (Complesso Universitario di Monte Sant’Angelo), Via Cintia, 80126 Napoli, Italy
Interests: protein crystallography; protein metalation; metallodrugs; protein–metal-based drug adducts; X-ray crystallography; protein–ligand interactions
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

A symposium titled “Peptide and Protein metalation” will be held in Naples, Italy, on 10–12 June 2025 (https://www.ppmnaples25.com/home). The symposium will bring together world-renowned scientists and be a great opportunity to discuss the latest advances in the field of the interaction between metal ions or metal complexes and peptides and proteins. Inspired by this congress, the International Journal of Molecular Science will publish a Special Issue celebrating this topic and, as Guest Editors, we would be glad to invite you to contribute with original, high-quality works. Communications, full papers, and review articles are encouraged for this Special Issue. All submissions will go through an impartial peer review process.

Submissions for this SI are open. The SI is due to be published in late 2026.

Prof. Dr. Antonello Merlino
Prof. Dr. Irene Russo Krauss
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 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. 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

  • metallodrugs
  • metal ions
  • metal complexes
  • metal–protein interaction
  • metal–peptide interaction

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Published Papers (1 paper)

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Research

11 pages, 1987 KB  
Article
Dirhodium Tetraacetate Binding to Lysozyme at Body Temperature
by Gabriella Tito, Giarita Ferraro and Antonello Merlino
Int. J. Mol. Sci. 2025, 26(14), 6582; https://doi.org/10.3390/ijms26146582 - 9 Jul 2025
Viewed by 313
Abstract
Paddlewheel dirhodium complexes are cytotoxic compounds that are also used as catalysts and in the formation of Rh-based artificial metalloenzymes. Low-temperature structures of adducts formed by the model protein hen egg white lysozyme (HEWL) with dirhodium tetraacetate ([Rh2(μ-O2CCH3 [...] Read more.
Paddlewheel dirhodium complexes are cytotoxic compounds that are also used as catalysts and in the formation of Rh-based artificial metalloenzymes. Low-temperature structures of adducts formed by the model protein hen egg white lysozyme (HEWL) with dirhodium tetraacetate ([Rh2(μ-O2CCH3)4]) when crystals of the protein were treated with the metal compound at 20 °C demonstrated that [Rh2(μ-O2CCH3)4] in part breaks down upon reaction with HEWL; dimeric Rh-Rh units bind the side chains of Asp18 and the C-terminal carboxylate, and monometallic fragments coordinate the side chains of Arg14 and His15 in 20% ethylene glycol, 0.100 M sodium acetate at pH 4.5 and 0.600 M sodium nitrate, while dimeric Rh-Rh units bind the side chains of Asn93 and Lys96, the C-terminal carboxylate and Asp101, with monometallic fragments that bind the side chains of Lys33 and His15 in 0.010 M HEPES pH 7.5 and 2.00 M sodium formate. To verify whether the binding of this metallodrug to proteins also occurs at body temperature, crystals of HEWL were grown in 0.010 M HEPES pH 7.5 and 2.00 M sodium formate at 37 °C and soaked with [Rh2(μ-O2CCH3)4] at the same temperature. X-ray diffraction data collected on these crystals at 37 °C demonstrate that [Rh2(μ-O2CCH3)4] reacts with proteins at body temperature. The structures of the Rh/HEWL adduct formed at 20 °C (obtained from data collected at 100 K) and at 37 °C under the same experimental conditions are very similar, with metal binding sites that are conserved. However, metal-containing fragment occupancy is higher in the structure obtained at 37 °C, suggesting a role of temperature in defining the protein metalation process. Full article
(This article belongs to the Special Issue Peptide and Protein Metalation)
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