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Interactions between Metal Complexes and Biomolecules

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

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 13404

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Special Issue Editors

Dr. Li-Jun Chen

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Guest Editor

Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia
Interests: supramolecular chemistry; self-assembly; molecular recognition; ion transport; coordination chemistry; metal–organic structures; biomolecules recognition

Dr. Chang Lei

E-Mail Website
Guest Editor

Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia
Interests: developing novel nanomaterials for bioanalysis and tissue regeneration; and their transactions to affordable commercial products to be used in real cases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Metal complexes are important materials that have the potential for programmable structures to be engineered with integrated properties.

They have attracted significant research interest both due to their aesthetically attractive structures and their appealing properties. Interactions between metal complexes and biomolecules including lipids, oligopeptides, nucleic acids, proteins, etc. comprise an important research area related to metal complexes and are important in chemistry, biology, medicine, pharmacy, nutrition, metabolism, and environmental science. Metal–biomolecule interactions endow metal complexes with potential applications ranging from sensing and bio-imaging to catalysis, drug delivery, chemotherapeutics, photo-therapeutics, theranostics and more. Many of these applications have been explored with different types of metal complexes, including simple organometallic compounds and metal coordination assemblies, offering insights into the future potential of these compounds for the investigation and treatment of human diseases.

In this Special Issue of Molecules devoted to "Interactions between Metal Complexes and Biomolecules", we warmly invite investigators to contribute original research articles or review articles that could stimulate continuing efforts to understand the metal–biomolecule interactions and develop new metal-complex-related systems that intact with biomolecules. Topics of interest for this Special Issue include, but are not limited to, the following:

The synthesis, characterisation, and applications of new metal complexes or assemblies that can target and probe a specific biomolecule or as potential biomolecular binding substrates;
Molecular mechanistic understanding of the interaction between biomolecules and metal complexes;
The incorporation of biomolecules into metal-related systems, as well as the development and application of biomolecule–metal hybrid structures.

Dr. Li-Jun Chen
Dr. Chang Lei
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 complexes
biomolecules
interaction
organometallic complexes
hybrid structures
self-assembly

Published Papers (7 papers)

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Research

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18 pages, 3508 KiB

Open AccessArticle

Role of Alginate Composition on Copper Ion Uptake in the Presence of Histidine or Beta-Amyloid

by Cynthia Regina Albrecht Mahl, Rogério Aparecido Bataglioli, Guilherme Bedeschi Calais, Thiago Bezerra Taketa and Marisa Masumi Beppu

Molecules 2022, 27(23), 8334; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27238334 - 29 Nov 2022

Cited by 1 | Viewed by 1352

Abstract

The anomalous interaction between metal ions and the peptide beta-amyloid is one of the hallmarks of Alzheimer’s disease. Metal-binding biopolymers, including polysaccharides, can elucidate the fundamental aspects of metal ions’ interactions with biological tissue and their interplay in Alzheimer’s disease. This work focuses on the role of the alginate composition on Cu(II) adsorption in the presence of histidine or β-amyloid, the peptide associated with the progression of Alzheimer’s disease. Alginate samples with different mannuronic/guluronic (M/G) ratios led to similar Cu(II) adsorption capacities, following the Langmuir isotherm and the pseudo-second-order adsorption kinetic models. Although the presence of histidine produced up to a 20% reduction in the copper adsorption capacity in guluronic-rich alginate samples (M/G~0.61), they presented stable bidentate chelation of the metallic ion. Chemical analyses (FTIR and XPS) demonstrated the role of hydroxyl and carboxyl groups in copper ion chelation, whereas both crystallinity and morphology analyses indicated the prevalence of histidine interaction with guluronic-rich alginate. Similar results were observed for Cu(II) adsorption in alginate beads in the presence of beta-amyloid and histidine, suggesting that the alginate/histidine system is a simple yet representative model to probe the application of biopolymers to metal ion uptake in the presence of biological competitors. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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14 pages, 1925 KiB

Open AccessArticle

Intramolecular Folding of PolyT Oligonucleotides Induced by Cooperative Binding of Silver(I) Ions

by Jinghua Hao, Dong Cao, Qiang Zhao, Dapeng Zhang and Hailin Wang

Molecules 2022, 27(22), 7842; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27227842 - 14 Nov 2022

Viewed by 1475

Abstract

Ag⁺-bridged T-Ag⁺-T was recently discovered in a Ag⁺-DNA nanowire crystal, but it was reported that Ag⁺ had little to no affinity to T nucleobases and T-rich oligonucleotides in solution. Therefore, the binding mode for the formation of this type of novel metallo base pair in solution is elusive. Herein, we demonstrate that Ag⁺ can interact with polyT oligonucleotides once the concentration of Ag⁺ in solution exceeds a threshold value. The threshold value is independent of the concentration of the polyT oligonucleotide but is inversely proportional to the length of the polyT oligonucleotide. The polyT oligonucleotides are intramolecularly folded due to their positively cooperative formation and the stack of T-Ag⁺-T base pairs, resulting in the 5′- and 3′-ends being in close proximity to each other. The intramolecular Ag⁺-folded polyT oligonucleotide has a higher thermal stability than the duplex and can be reversibly modulated by cysteine. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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11 pages, 781 KiB

Open AccessCommunication

Alteration of Biomolecular Conformation by Aluminum-Implications for Protein Misfolding Disease

by Yuhai Zhao, Aileen I. Pogue, Peter N. Alexandrov, Leslie G. Butler, Wenhong Li, Vivian R. Jaber and Walter J. Lukiw

Molecules 2022, 27(16), 5123; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27165123 - 11 Aug 2022

Cited by 2 | Viewed by 1788

Abstract

The natural element aluminum possesses a number of unique biochemical and biophysical properties that make this highly neurotoxic species deleterious towards the structural integrity, conformation, reactivity and stability of several important biomolecules. These include aluminum’s (i) small ionic size and highly electrophilic nature, having the highest charge density of any metallic cation with a Z²/r of 18 (ionic charge +3, radius 0.5 nm); (ii) inclination to form extremely stable electrostatic bonds with a tendency towards covalency; (iii) ability to interact irreversibly and/or significantly slow down the exchange-rates of complex aluminum–biomolecular interactions; (iv) extremely dense electropositive charge with one of the highest known affinities for oxygen-donor ligands such as phosphate; (v) presence as the most abundant metal in the Earth’s biosphere and general bioavailability in drinking water, food, medicines, consumer products, groundwater and atmospheric dust; and (vi) abundance as one of the most commonly encountered intracellular and extracellular metallotoxins. Despite aluminum’s prevalence and abundance in the biosphere it is remarkably well-tolerated by all plant and animal species; no organism is known to utilize aluminum metabolically; however, a biological role for aluminum has been assigned in the compaction of chromatin. In this Communication, several examples are given where aluminum has been shown to irreversibly perturb and/or stabilize the natural conformation of biomolecules known to be important in energy metabolism, gene expression, cellular homeostasis and pathological signaling in neurological disease. Several neurodegenerative disorders that include the tauopathies, Alzheimer’s disease and multiple prion disorders involve the altered conformation of naturally occurring cellular proteins. Based on the data currently available we speculate that one way aluminum contributes to neurological disease is to induce the misfolding of naturally occurring proteins into altered pathological configurations that contribute to the neurodegenerative disease process. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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16 pages, 6340 KiB

Open AccessArticle

Supramolecular Hybrids from Cyanometallate Complexes and Diblock Copolypeptide Amphiphiles in Water

by Takayuki Tanaka and Keita Kuroiwa

Molecules 2022, 27(10), 3262; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27103262 - 19 May 2022

Cited by 1 | Viewed by 1284

Abstract

The self-assembly of discrete cyanometallates has attracted significant interest due to the potential of these materials to undergo soft metallophilic interactions as well as their optical properties. Diblock copolypeptide amphiphiles have also been investigated concerning their capacity for self-assembly into morphologies such as nanostructures. The present work combined these two concepts by examining supramolecular hybrids comprising cyanometallates with diblock copolypeptide amphiphiles in aqueous solutions. Discrete cyanometallates such as [Au(CN)₂]⁻, [Ag(CN)₂]⁻, and [Pt(CN)₄]²⁻ dispersed at the molecular level in water cannot interact with each other at low concentrations. However, the results of this work demonstrate that the addition of diblock copolypeptide amphiphiles such as poly-(L-lysine)-block-(L-cysteine) (Lys_m-b-Cys_n) to solutions of these complexes induces the supramolecular assembly of the discrete cyanometallates, resulting in photoluminescence originating from multinuclear complexes with metal-metal interactions. Electron microscopy images confirmed the formation of nanostructures of several hundred nanometers in size that grew to form advanced nanoarchitectures, including those resembling the original nanostructures. This concept of combining diblock copolypeptide amphiphiles with discrete cyanometallates allows the design of flexible and functional supramolecular hybrid systems in water. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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12 pages, 21846 KiB

Open AccessArticle

Biomineralization of Nickel Struvite Linked to Metal Resistance in Streptomyces mirabilis

by Flávio Silva Costa, Falko Langenhorst and Erika Kothe

Molecules 2022, 27(10), 3061; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27103061 - 10 May 2022

Cited by 3 | Viewed by 1458

Abstract

Biomineral formation is a common trait and prominent for soil Actinobacteria, including the genus Streptomyces. We investigated the formation of nickel-containing biominerals in the presence of a heavy-metal-resistant Streptomyces mirabilis P16B-1. Biomineralization was found to occur both in solid and liquid media. Minerals were identified with Raman spectroscopy and TEM-EDX to be either Mg-containing struvite produced in media containing no nickel, or Ni-struvite where Ni replaces the Mg when nickel was present in sufficient concentrations in the media. The precipitation of Ni-struvite reduced the concentration of nickel available in the medium. Therefore, Ni-struvite precipitation is an efficient mechanism for tolerance to nickel. We discuss the contribution of a plasmid-encoded nickel efflux transporter in aiding biomineralization. In the elevated local concentrations of Ni surrounding the cells carrying this plasmid, more biominerals occurred supporting this point of view. The biominerals formed have been quantified, showing that the conditions of growth do influence mineralization. This control is also visible in differences observed to biosynthetically synthesized Ni-struvites, including the use of sterile-filtered culture supernatant. The use of the wildtype S. mirabilis P16B-1 and its plasmid-free derivative, as well as a metal-sensitive recipient, S. lividans, and the same transformed with the plasmid, allowed us to access genetic factors involved in this partial control of biomineral formation. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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15 pages, 2679 KiB

Open AccessArticle

Zinc and Copper Ions Induce Aggregation of Human β-Crystallins

by Vanesa Ramirez-Bello, Javier Martinez-Seoane, Arline Fernández-Silva and Carlos Amero

Molecules 2022, 27(9), 2970; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27092970 - 06 May 2022

Cited by 6 | Viewed by 2049

Abstract

Cataracts are defined as the clouding of the lens due to the formation of insoluble protein aggregates. Metal ions exposure has been recognized as a risk factor in the cataract formation process. The γ and β crystallins are members of a larger family and share several structural features. Several studies have shown that copper and zinc ions induce the formation of γ-crystallins aggregates. However, the interaction of metal ions with β-crystallins, some of the most abundant crystallins in the lens, has not been explored until now. Here, we evaluate the effect of Cu(II) and Zn(II) ions on the aggregation of HβA1, as a representative of the acidic form, and HβB2, as a representative of the basic β-crystallins. We used several biophysical techniques and computational methods to show that Cu(II) and Zn(II) induce aggregation following different pathways. Both metal ions destabilize the proteins and impact protein folding. Copper induced a small conformational change in HβA1, leading to high-molecular-weight light-scattering aggregates, while zinc is more aggressive towards HβB2 and induces a larger conformational change. Our work provides information on the mechanisms of metal-induced aggregation of β-crystallins. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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Review

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17 pages, 4410 KiB

Open AccessFeature PaperReview

Low-Molecular-Weight Fe(III) Complexes for MRI Contrast Agents

by Shangjun Chen, Lu An and Shiping Yang

Molecules 2022, 27(14), 4573; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27144573 - 18 Jul 2022

Cited by 6 | Viewed by 3034

Abstract

Fe(III) complexes have again attracted much attention for application as MRI contrast agents in recent years due to their high thermodynamic stability, low long-term toxicity, and large relaxivity at a higher magnetic field. This mini-review covers the recent progress on low-molecular-weight Fe(III) complexes, which have been considered as one of the promising alternatives to clinically used Gd(III)-based contrast agents. Two kinds of complexes including mononuclear Fe(III) complexes and multinuclear Fe(III) complexes are summarized in sequence, with a specific highlight of the structural relationships between the complexes and their relaxivity and thermodynamic stability. In additional, the future perspectives for the design of low-molecular-weight Fe(III) complexes for MRI contrast agents are suggested. Full article

(This article belongs to the Special Issue Interactions between Metal Complexes and Biomolecules)

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