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Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools

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

Deadline for manuscript submissions: 30 June 2024 | Viewed by 6813

Special Issue Editors

Dr. Andre Silva

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Guest Editor
LAQV-REQUIMTE, Departmento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto, Porto, Portugal
Interests: inorganic biochemistry; metal ions in biology; iron biochemistry; protein post-translational modifications
Special Issues, Collections and Topics in MDPI journals
Dr. Maria Rangel

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Guest Editor
LAQV/REQUIMTE, Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, 4099-003 Porto, Portugal
Interests: bioinorganic chemistry; metal ions in biology; iron chelators; EPR spectroscopy; membranes
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Transition metal ions are essential for life. Metalloenzymes correspond to over a third of all enzymes, and they play an essential role in fundamental biological processes such as DNA synthesis and replication, oxygen transport, mitochondrial respiration, and photosynthesis. However, there is an inherent toxicity problem which emanates from intrinsic reactivity under biological conditions. In order to prevent the deleterious effects resulting either from the deficit of these micronutrients or their toxic surplus, organisms have to tightly regulate metal ion levels and control their speciation in different compartments. In higher organisms (animals and plants) this tight regulation also means controlling both transport to the various organs and bioavailability to different tissues and cells.

In addition, several metal ion chelates (i.e., metallodrugs) are used as medicines and supplements, such as some radiopharmaceuticals, insulin mimetic drugs and iron formulations to fight anemia. An important step in comprehending their safety and efficacy is to realize their stability, distribution, and association with proteins in biological fluids. In this context, having a clear understanding about metal ion ligands, stability constants and redox potentials may provide the means to identify important cellular pathways and biochemical regulatory mechanisms.

This Special Issue of Molecules is dedicated to original research and review articles in the areas of inorganic biochemistry and bioinorganic chemistry. We aim to cover the latest findings on metal ion chemistry in biological systems as well as possible applications of such knowledge for the promotion of wellbeing. We will welcome studies employing chemical, molecular and spectroscopic tools to provide relevant insights for biological conditions. Results concerning speciation, redox activity, protein binding or how protein expression levels or modifications influence metal ion distribution or bioavailability will be accepted. Descriptions of quantification methods for individual species by chemical or spectroscopic methods will also be considered.

Dr. Andre Silva
Dr. Maria Rangel
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. Molecules is an international peer-reviewed open access semimonthly 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

  • metal ion speciation
  • metal ion complex stability
  • metallodrugs
  • metal ion chelates
  • chelators
  • protein binding
  • protein modifications
  • spectroscopy
  • stability constant

Published Papers (6 papers)

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Research

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22 pages, 2647 KiB  
Article
In Vivo Trafficking of the Anticancer Drug Tris(8-Quinolinolato) Gallium (III) (KP46) by Gallium-68/67 PET/SPECT Imaging
by Afnan M. F. Darwesh, Cinzia Imberti, Joanna J. Bartnicka, Fahad Al-Salemee, Julia E. Blower, Alex Rigby, Jayanta Bordoloi, Alex Griffiths, Michelle T. Ma and Philip J. Blower
Molecules 2023, 28(20), 7217; https://doi.org/10.3390/molecules28207217 - 22 Oct 2023
Viewed by 1074
Abstract
KP46 (tris(hydroxyquinolinato)gallium(III)) is an experimental, orally administered anticancer drug. Its absorption, delivery to tumours, and mode of action are poorly understood. We aimed to gain insight into these issues using gallium-67 and gallium-68 as radiotracers with SPECT and PET imaging in mice. [ [...] Read more.
KP46 (tris(hydroxyquinolinato)gallium(III)) is an experimental, orally administered anticancer drug. Its absorption, delivery to tumours, and mode of action are poorly understood. We aimed to gain insight into these issues using gallium-67 and gallium-68 as radiotracers with SPECT and PET imaging in mice. [67Ga]KP46 and [68Ga]KP46, compared with [68Ga]gallium acetate, were used for logP measurements, in vitro cell uptake studies in A375 melanoma cells, and in vivo imaging in mice bearing A375 tumour xenografts up to 48 h after intravenous (tracer level) and oral (tracer and bulk) administration. 68Ga was more efficiently accumulated in A375 cells in vitro when presented as [68Ga]KP46 than as [68Ga]gallium acetate, but the reverse was observed when intravenously administered in vivo. After oral administration of [68/67Ga]KP46, absorption of 68Ga and 67Ga from the GI tract and delivery to tumours were poor, with the majority excreted in faeces. By 48 h, low but measurable amounts were accumulated in tumours. The distribution in tissues of absorbed radiogallium and octanol extraction of tissues suggested trafficking as free gallium rather than as KP46. We conclude that KP46 likely acts as a slow releaser of gallium ions which are inefficiently absorbed from the GI tract and trafficked to tissues, including tumour and bone. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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16 pages, 4677 KiB  
Article
N-Acetylcysteine Displaces Glutathionyl-Moieties from Hg2+ and MeHg+ to Form More Hydrophobic Complexes at Near-Physiological Conditions
by Maryam Doroudian, Michelle E. Thibault and Jürgen Gailer
Molecules 2023, 28(19), 6762; https://doi.org/10.3390/molecules28196762 - 22 Sep 2023
Cited by 1 | Viewed by 740
Abstract
The anthropogenic release of Hg is associated with an increased human exposure risk. Since Hg2+ and MeHg+ have a high affinity for thiols, their interaction with L-glutathione (GSH) within mammalian cells is fundamentally involved in their toxicological chemistry and excretion. To [...] Read more.
The anthropogenic release of Hg is associated with an increased human exposure risk. Since Hg2+ and MeHg+ have a high affinity for thiols, their interaction with L-glutathione (GSH) within mammalian cells is fundamentally involved in their toxicological chemistry and excretion. To gain insight into the interaction of these mercurials with multiple small molecular weight thiols, we have investigated their competitive interactions with GSH and N-acetylcysteine (NAC) at near-physiological conditions, using a liquid chromatographic approach. This approach involved the injection of each mercurial onto a reversed-phase (RP)-HPLC column (37 °C) using a PBS buffer mobile phase containing 5.0 mM GSH to simulate cytosolic conditions with Hg being detected in the column effluent by an inductively coupled plasma atomic emission spectrometer (ICP-AES). When the 5.0 mM GSH mobile phase was amended with up to 10 mM NAC, gradually increasing retention times of both mercurials were observed. To explain this behavior, the experiment with 5.0 mM NAC and 5.0 mM GSH was replicated using 50 mM Tris buffer (pH 7.4), and the Hg-containing fractions were analyzed by electrospray ionization mass spectrometry. The results revealed the presence of Hg(GS)(NAC) and Hg(NAC)2 for Hg2+ and MeHg(GS) and MeHg(NAC) for MeHg+, which suggests that the coordination/displacement of GS-moieties from each mercurial by the more hydrophobic NAC can explain their retention behavior. Since the biotransformations of both mercurials were observed at near-physiological conditions, they are of toxicological relevance as they provide a biomolecular explanation for some results that were obtained when animals were administered with each mercurial and NAC. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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15 pages, 4670 KiB  
Article
A Combined NMR and UV–Vis Approach to Evaluate Radical Scavenging Activity of Rosmarinic Acid and Other Polyphenols
by Arian Kola, Ginevra Vigni, Maria Camilla Baratto and Daniela Valensin
Molecules 2023, 28(18), 6629; https://doi.org/10.3390/molecules28186629 - 14 Sep 2023
Cited by 1 | Viewed by 861
Abstract
Oxidative stress results from an imbalance between reactive oxygen species (ROS) production and the body’s ability to neutralize them. ROS are reactive molecules generated during cellular metabolism and play a crucial role in normal physiological processes. However, excessive ROS production can lead to [...] Read more.
Oxidative stress results from an imbalance between reactive oxygen species (ROS) production and the body’s ability to neutralize them. ROS are reactive molecules generated during cellular metabolism and play a crucial role in normal physiological processes. However, excessive ROS production can lead to oxidative damage, contributing to various diseases and aging. This study is focused on rosmarinic acid (RA), a hydroxycinnamic acid (HCA) derivative well known for its antioxidant activity. In addition, RA has also demonstrated prooxidant behavior under specific conditions involving high concentrations of transition metal ions such as iron and copper, high pH, and the presence of oxygen. In this study, we aim to clarify the underlying mechanisms and factors governing the antioxidant and prooxidant activities of RA, and to compare them with other HCA derivatives. UV–Vis, NMR, and EPR techniques were used to explore copper(II)’s binding ability of RA, caffeic acid, and p-coumaric acid. At the same time, UV–Vis and NMR methods were exploited to evaluate the polyphenols’ free radical scavenging abilities towards ROS generated by the ascorbic acid–copper(II) system. All the data indicate that RA is the most effective polyphenol both in copper binding abilities and ROS protection. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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14 pages, 2753 KiB  
Article
Modulation Effects of Fe3+, Zn2+, and Cu2+ Ions on the Amyloid Fibrillation of α-Synuclein: Insights from a FTIR Investigation
by Yan Li, Yang Yu and Gang Ma
Molecules 2022, 27(23), 8383; https://doi.org/10.3390/molecules27238383 - 01 Dec 2022
Cited by 4 | Viewed by 1287
Abstract
Amyloid fibrillation of α-synuclein is implicated in the pathogenesis of Parkinson’s disease and heavy metal ions such as Fe3+, Zn2+, and Cu2+ are known to be involved in the process. In this work, we explored the use of [...] Read more.
Amyloid fibrillation of α-synuclein is implicated in the pathogenesis of Parkinson’s disease and heavy metal ions such as Fe3+, Zn2+, and Cu2+ are known to be involved in the process. In this work, we explored the use of FTIR spectroscopy to look into the modulation effects of Fe3+, Zn2+, and Cu2+ on the amyloid fibrillation of α-synuclein. We performed a curve-fitting analysis on the FTIR amide I bands of these α-synuclein fibril systems, namely, the pristine fibril and the fibrils prepared in the presence of Fe3+, Zn2+, and Cu2+. We found that the α-synuclein fibrils under the influences of metal ions all possessed a parallel β-sheet structure, turn structure, and disordered structure, similar to that of pristine α-synuclein fibril. We also observed metal-induced increases in the proportions of the β-sheet secondary structure within the α-synuclein fibrils, with Fe3+ being the most effective inducer. We performed second derivative analysis of the side chain carboxylic groups of α-synuclein fibrils and found that the side chain microenvironment of the α-synuclein fibrils was more influenced by Fe3+ than Zn2+, and Cu2+. In addition, our atomic force microscopic study revealed that the morphologies of α-synuclein fibrils under the influence of Fe3+ was quite different from that of the Zn2+ and Cu2+ systems. Our FTIR results suggested that the modulation effects of Fe3+, Zn2+, and Cu2+ on α-synuclein fibrillation occurred at both secondary and quaternary structural levels. At last, we proposed a mechanistic hypothesis to interpret how metal ions could affect the morphology of α-synuclein amyloid fibril based on the conformational plasticity properties of intrinsically disordered proteins. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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Review

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16 pages, 1767 KiB  
Review
New Perspectives on Circulating Ferritin: Its Role in Health and Disease
by Óscar Fonseca, Ana S. Ramos, Leonor T. S. Gomes, Maria Salomé Gomes and Ana C. Moreira
Molecules 2023, 28(23), 7707; https://doi.org/10.3390/molecules28237707 - 22 Nov 2023
Viewed by 1380
Abstract
The diagnosis of iron disturbances usually includes the evaluation of serum parameters. Serum iron is assumed to be entirely bound to transferrin, and transferrin saturation—the ratio between the serum iron concentration and serum transferrin—usually reflects iron availability. Additionally, serum ferritin is commonly used [...] Read more.
The diagnosis of iron disturbances usually includes the evaluation of serum parameters. Serum iron is assumed to be entirely bound to transferrin, and transferrin saturation—the ratio between the serum iron concentration and serum transferrin—usually reflects iron availability. Additionally, serum ferritin is commonly used as a surrogate of tissue iron levels. Low serum ferritin values are interpreted as a sign of iron deficiency, and high values are the main indicator of pathological iron overload. However, in situations of inflammation, serum ferritin levels may be very high, independently of tissue iron levels. This presents a particularly puzzling challenge for the clinician evaluating the overall iron status of the patient in the presence of an inflammatory condition. The increase in serum ferritin during inflammation is one of the enigmas regarding iron metabolism. Neither the origin, the mechanism of release, nor the effects of serum ferritin are known. The use of serum ferritin as a biomarker of disease has been rising, and it has become increasingly diverse, but whether or not it contributes to controlling the disease or host pathology, and how it would do it, are important, open questions. These will be discussed here, where we spotlight circulating ferritin and revise the recent clinical and preclinical data regarding its role in health and disease. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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21 pages, 9895 KiB  
Review
Optical Imaging Opportunities to Inspect the Nature of Cytosolic Iron Pools
by Robert Charles Hider, Charareh Pourzand, Yongmin Ma and Agostino Cilibrizzi
Molecules 2023, 28(18), 6467; https://doi.org/10.3390/molecules28186467 - 06 Sep 2023
Cited by 1 | Viewed by 843
Abstract
The chemical nature of intracellular labile iron pools (LIPs) is described. By virtue of the kinetic lability of these pools, it is suggested that the isolation of such species by chromatography methods will not be possible, but rather mass spectrometric techniques should be [...] Read more.
The chemical nature of intracellular labile iron pools (LIPs) is described. By virtue of the kinetic lability of these pools, it is suggested that the isolation of such species by chromatography methods will not be possible, but rather mass spectrometric techniques should be adopted. Iron-sensitive fluorescent probes, which have been developed for the detection and quantification of LIP, are described, including those specifically designed to monitor cytosolic, mitochondrial, and lysosomal LIPs. The potential of near-infrared (NIR) probes for in vivo monitoring of LIP is discussed. Full article
(This article belongs to the Special Issue Metal Ions in Biology and Health: Insights from Molecular and Spectroscopic Tools)
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