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Metals in Biology and Medicine

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

Deadline for manuscript submissions: closed (20 October 2024) | Viewed by 3734

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Guest Editor
Faculty of Chemistry and Pharmacy, Sofia University “St. Kliment Ohridski”, 1164 Sofia, Bulgaria
Interests: computational chemistry/biochemistry/biophysics; molecular modeling; metals in biology and medicine
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Special Issue Information

Dear Colleagues, 

Almost half of all known proteins contain metal cations. Over the course of organism   evolution, specific biological functions have been bestowed upon several (biogenic) metal species, with Na+, K+, Mg2+, Ca2+, Zn2+, Mn2+/3+, Fe2+/3+, Cu+/2+ and Co2+/3+ found the most frequently.

The high-fidelity selection of the native metal cation from the surrounding fluids that teem with other contending metal species is of paramount importance for the faultless functioning of metalloproteins. Several highly efficient strategies have been developed by the host protein or cell machinery that enable the native metal cofactor to outdo its rivals in binding the target protein. The safeguard system of the protein, however, has not evolved sufficiently well to effectively thwart attacks by foreign (abiogenic) metal cations which were excluded from the evolutionary process, such as Hg2+, Pb2+, Al3+, Cd2+, Li+, Ag+, Sr2+, Ga3+, La3+ and many others. These are not under homeostatic control and, after eluding the host organism’s defense system and competing with native metal species, may adversely affect specific biochemical processes, thus intoxicating the recipient (e.g. mercury, cadmium or lead poisoning). In particular circumstances, however, the substitution of the native cation by an “alien” competitor might appear advantageous for the host organism. Such “friendly” abiogenic metal cations help humans to successfully cope with medical conditions such as psychiatric disorders (Li+), osteoporosis (Sr2+), tumor formations (Sr2+, Ga3+) and bacterial infections (Ag+, Ga3+). The mechanisms of the abiogenic metal cations’ “friendly” or “unfriendly” behaviour, however, are not well understood and many questions remain.

Thus, we kindly invite you to contribute a full-length paper or a review article to this Special Issue, which will focus on the role that both biogenic and abiogenic metals play in human pathogenesis or medical care. This information will be beneficial to a large audience of scientists and practitioners working in the field.

Prof. Dr. Todor Dudev
Guest Editor

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Keywords

  • biogenic/abiogenic metal cations
  • metal binding/selectivity
  • metalloproteins
  • enzymes
  • metal toxicity
  • health-beneficial effect

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Published Papers (2 papers)

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Research

13 pages, 1843 KiB  
Article
Cobalt(II) and Manganese(II) Complexes of Sodium Monensinate A Bearing Nitrate Co-Ligands
by Nikolay Petkov, Miroslav Boyadzhiev, Nikita Bozhilova, Petar Dorkov, Elzhana Encheva, Angel Ugrinov and Ivayla N. Pantcheva
Int. J. Mol. Sci. 2024, 25(22), 12129; https://doi.org/10.3390/ijms252212129 - 12 Nov 2024
Viewed by 421
Abstract
Monensic acid is a natural polyether ionophore and is a therapeutic of first choice in veterinary medicine for the control of coccidiosis. Although known as a sodium-binding ligand, it can also form a variety of coordination species depending on experimental conditions applied. In [...] Read more.
Monensic acid is a natural polyether ionophore and is a therapeutic of first choice in veterinary medicine for the control of coccidiosis. Although known as a sodium-binding ligand, it can also form a variety of coordination species depending on experimental conditions applied. In this study, we present the crystal structures and properties of Co(II) and Mn(II) complexes of sodium monensinate (MonNa) derived from the reaction of MonNa with cobalt or manganese dinitrates. The newly obtained coordination compounds have the same composition [M(MonNa)2(NO3)2] but the transition metal ions are placed in a different environment. The two nitrate ligands behave mono- or bidentately bound in the Co(II)- and Mn(II)-containing species, respectively, while the monensinate ligands act in a similar manner through their monodentate carboxylate functions. The formed CoO4 and MnO6 units determine the geometry of the corresponding inner coordination cores of the complexes as a tetrahedron in the case of Co(II), and as a strongly distorted octahedral structure in Mn(II) species. The effect of inorganic anions on the antibacterial performance of sodium monensinate appears to be negligible, while the presence of Co(II) or Mn(II) cations preserves or enhances the activity of unmodified MonNa, which differentially affects the growth of Bacillus subtilis, Bacillus cereus, Kocuria rhizophila, Staphilococcus aureus, and Staphilococcus saprophyticus strains. Full article
(This article belongs to the Special Issue Metals in Biology and Medicine)
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13 pages, 1655 KiB  
Article
Lanthanides as Calcium Mimetic Species in Calcium-Signaling/Buffering Proteins: The Effect of Lanthanide Type on the Ca2+/Ln3+ Competition
by Valya Nikolova, Nikoleta Kircheva, Stefan Dobrev, Silvia Angelova and Todor Dudev
Int. J. Mol. Sci. 2023, 24(7), 6297; https://doi.org/10.3390/ijms24076297 - 27 Mar 2023
Cited by 12 | Viewed by 2173
Abstract
Lanthanides, the 14 4f-block elements plus Lanthanum, have been extensively used to study the structure and biochemical properties of metalloproteins. The characteristics of lanthanides within the lanthanide series are similar, but not identical. The present research offers a systematic investigation of the ability [...] Read more.
Lanthanides, the 14 4f-block elements plus Lanthanum, have been extensively used to study the structure and biochemical properties of metalloproteins. The characteristics of lanthanides within the lanthanide series are similar, but not identical. The present research offers a systematic investigation of the ability of the entire Ln3+ series to substitute for Ca2+ in biological systems. A well-calibrated DFT/PCM protocol is employed in studying the factors that control the metal selectivity in biological systems by modeling typical calcium signaling/buffering binding sites and elucidating the thermodynamic outcome of the competition between the “alien” La3+/Ln3+ and “native” Ca2+, and La3+ − Ln3+ within the lanthanide series. The calculations performed reveal that the major determinant of the Ca2+/Ln3+ selectivity in calcium proteins is the net charge of the calcium binding pocket; the more negative the charge, the higher the competitiveness of the trivalent Ln3+ with respect to its Ca2+ contender. Solvent exposure of the binding site also influences the process; buried active centers with net charge of −4 or −3 are characterized by higher Ln3+ over Ca2+ selectivity, whereas it is the opposite for sites with overall charge of −1. Within the series, the competition between La3+ and its fellow lanthanides is determined by the balance between two competing effects: electronic (favoring heavier lanthanides) and solvation (generally favoring the lighter lanthanides). Full article
(This article belongs to the Special Issue Metals in Biology and Medicine)
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