The specific interactions of anionic metal-oxo clusters, known as polyoxometalates (POMs), with proteins can be leveraged for a wide range of analytical and biomedical applications. For example, POMs have been developed as selective catalysts that can induce protein modifications and have also been shown to facilitate protein crystallization, both of which are instrumental in the structural characterization of proteins. POMs can also be used for selective protein separation and enzyme inhibition, which makes them promising therapeutic agents. Hence, understanding POM-protein interactions is essential for the development of POM-based materials and their implementation in several fields. In this Review we summarize in detail the key insights that have been gained so far on POM-protein interactions. Emphasis is also given to hybrid POMs functionalized with organic ligands to prompt further research in this direction owing to the promising recent results on tuning POM-protein interactions through POM functionalization.
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Exploiting Interactions between Polyoxometalates and Proteins for Applications in (Bio)chemistry and Medicine.
Angew Chem Int Ed Engl
August 2023
Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001, Leuven, Belgium.
The specific interactions of anionic metal-oxo clusters, known as polyoxometalates (POMs), with proteins can be leveraged for a wide range of analytical and biomedical applications. For example, POMs have been developed as selective catalysts that can induce protein modifications and have also been shown to facilitate protein crystallization, both of which are instrumental in the structural characterization of proteins. POMs can also be used for selective protein separation and enzyme inhibition, which makes them promising therapeutic agents.
View Article and Find Full Text PDFComputational Modelling of the Interactions Between Polyoxometalates and Biological Systems.
Front Chem
April 2022
Department de Química Física i Inorgànica, Universitat Rovira i Virgili, Tarragona, Spain.
Polyoxometalates (POMs) structures have raised considerable interest for the last years in their application to biological processes and medicine. Within this area, our mini-review shows that computational modelling is an emerging tool, which can play an important role in understanding the interaction of POMs with biological systems and the mechanisms responsible of their activity, otherwise difficult to achieve experimentally. During recent years, computational studies have mainly focused on the analysis of POM binding to proteins and other systems such as lipid bilayers and nucleic acids, and on the characterization of reaction mechanisms of POMs acting as artificial metalloproteases and phosphoesterases.
View Article and Find Full Text PDFSynthesis, characterization, and POM-protein interactions of a Fe-substituted Krebs-type Sandwich-tungstoantimonate.
Monatsh Chem
April 2019
1Universität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090 Wien, Austria.
Abstract: The novel iron-substituted Krebs-type polyoxotungstate (CNH)NaH[(Fe(HO))((FeO)(WO))(β-SbWO)] () has been synthesized using -phenylenediamine (opda) as a precursor for the in situ formation of the counter cation 2,3-diaminophenazinium (CNH) (2,3-DAP). has been thoroughly characterized in the solid state by single-crystal X-ray diffraction (SXRD), powder X-ray diffraction (PXRD), IR spectroscopy, and elemental analysis as well as in solution by UV-Vis spectroscopy. The crystal structure of reveals -interactions between the aromatic systems of the unconventional 2,3-DAP counter cation.
View Article and Find Full Text PDFSelective Hydrolysis of Ovalbumin Promoted by Hf(IV)-Substituted Wells-Dawson-Type Polyoxometalate.
Front Chem
December 2018
Laboratory of Bio-Inorganic Chemistry, Department of Chemistry, KU Leuven, Leuven, Belgium.
The reactivity and selectivity of Wells-Dawson type polyoxometalate (POM), K[Hf(α-PWO)]·19HO (Hf1-WD2), have been examined with respect to the hydrolysis of ovalbumin (OVA), a storage protein consisting of 385 amino acids. The exact cleavage sites have been determined by Edman degradation experiments, which indicated that Hf1-WD2 POM selectively cleaved OVA at eight peptide bonds: Phe13-Asp14, Arg85-Asp86, Asn95-Asp96, Ala139-Asp140, Ser148-Trp149, Ala361-Asp362, Asp362-His363, and Pro364-Phe365. A combination of spectroscopic methods including P NMR, Circular Dichroism (CD), and Tryptophan (Trp) fluorescence spectroscopy were employed to gain better understanding of the observed selective cleavage and the underlying hydrolytic mechanism.
View Article and Find Full Text PDFThe antibacterial activity of polyoxometalates: structures, antibiotic effects and future perspectives.
Chem Commun (Camb)
January 2018
Universität Wien, Fakultät für Chemie, Institut für Biophysikalische Chemie, Althanstraße 14, 1090 Wien, Austria.
Polyoxometalates (POMs) are, mostly anionic, metal oxide compounds that span a wide range of tunable physical and chemical features rendering them very interesting for biological purposes, an continuously emerging but little explored field. Due to their biological and biochemical effects, including antitumor, -viral and -bacterial properties, POMs and POM-based systems are considered as promising future metallodrugs. In this article, we focus on the antibacterial activity of POMs and their therapeutic potential in the battle against bacteria and their increasing resistance against pharmaceuticals.
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