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Special Issue "Interaction between Metal Compounds and Proteins"

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 (15 January 2019)

Special Issue Editor

Guest Editor
Prof. Antonello Merlino

Department of Chemical Sciences, University of Naples Federico II, Napoli, Italy
Website | E-Mail
Interests: protein–metal-based drug adducts; X-Ray crystallography; protein metalation; protein–ligand interactions

Special Issue Information

Dear colleagues,

The binding of metal compounds to proteins plays a major role in many different fields of chemistry, from drug delivery to catalysis, from the biotechnological applications of natural and synthetic metalloenzymes to the definition of the pharmacological profiles of drugs. Here, we plan to collect original research articles, short communications, or review articles describing recent advances in the field of the characterization of the interactions between proteins and metal compounds, including metal nanoparticles.

Potential topics include, but are not limited to, the following:

Mechanistic studies of the protein metalation process

Analytical advances in the identification of protein targets for metallodrugs

Analytical advances in the determination of protein–metal recognition binding sites

Structural data on the formation of protein–metal adducts and protein–metal complexes

Identification of metal binding sites on protein structures

Biophysical studies of the interactions between proteins and metal nanoclusters/nanoparticles

Prof. Antonello Merlino
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. International Journal of Molecular Sciences is an international peer-reviewed open access bimonthly 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.


  • Protein–metal adducts
  • Protein metalation
  • Protein–metal nanoparticle interactions
  • Metal binding sites
  • Metallomics
  • Organometallic compounds
  • Metal-based drugs
  • Metalloenzymes

Published Papers (1 paper)

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Open AccessArticle Copper Binding Features of Tropomyosin-Receptor-Kinase-A Fragment: Clue for Neurotrophic Factors and Metals Link
Int. J. Mol. Sci. 2018, 19(8), 2374; https://doi.org/10.3390/ijms19082374
Received: 30 June 2018 / Revised: 1 August 2018 / Accepted: 7 August 2018 / Published: 12 August 2018
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The nerve growth factor (NGF) is a neurotrophin essential for the development and maintenance of neurons, whose activity is influenced by copper ions. The NGF protein exerts its action by binding to its specific receptor, TrkA. In this study, a specific domain of
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The nerve growth factor (NGF) is a neurotrophin essential for the development and maintenance of neurons, whose activity is influenced by copper ions. The NGF protein exerts its action by binding to its specific receptor, TrkA. In this study, a specific domain of the TrkA receptor, region 58–64, was synthesized and its copper(II) complexes characterized by means of potentiometric and spectroscopic studies. The two vicinal histidine residues provide excellent metal anchoring sites and, at physiological pH, a complex with the involvement of the peptide backbone amide nitrogen is the predominant species. The TrkA peptide is competitive for metal binding with analogous peptides due to the N-terminal domain of NGF. These data provide cues for future exploration of the effect of metal ions on the activity of the NGF and its specific cellular receptor. Full article
(This article belongs to the Special Issue Interaction between Metal Compounds and Proteins)

Graphical abstract

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
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