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Article

Antimicrobial Activity of Rhenium Di- and Tricarbonyl Diimine Complexes: Insights on Membrane-Bound S. aureus Protein Binding

1
Department of Chemistry, Fribourg University, Chemin Du Musée 9, 1700 Fribourg, Switzerland
2
Institute of Molecular Genetics and Genetic Engineering, University of Belgrade, Vojvode Stepe 444a, 11042 Belgrade, Serbia
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editors: Fiorella Meneghetti and Daniela Barlocco
Pharmaceuticals 2022, 15(9), 1107; https://doi.org/10.3390/ph15091107
Received: 4 August 2022 / Revised: 31 August 2022 / Accepted: 31 August 2022 / Published: 5 September 2022
(This article belongs to the Special Issue Novel Antibacterial Agents 2022)
Antimicrobial resistance is one of the major human health threats, with significant impacts on the global economy. Antibiotics are becoming increasingly ineffective as drug-resistance spreads, imposing an urgent need for new and innovative antimicrobial agents. Metal complexes are an untapped source of antimicrobial potential. Rhenium complexes, amongst others, are particularly attractive due to their low in vivo toxicity and high antimicrobial activity, but little is known about their targets and mechanism of action. In this study, a series of rhenium di- and tricarbonyl diimine complexes were prepared and evaluated for their antimicrobial potential against eight different microorganisms comprising Gram-negative and -positive bacteria. Our data showed that none of the Re dicarbonyl or neutral tricarbonyl species have either bactericidal or bacteriostatic potential. In order to identify possible targets of the molecules, and thus possibly understand the observed differences in the antimicrobial efficacy of the molecules, we computationally evaluated the binding affinity of active and inactive complexes against structurally characterized membrane-bound S. aureus proteins. The computational analysis indicates two possible major targets for this class of compounds, namely lipoteichoic acids flippase (LtaA) and lipoprotein signal peptidase II (LspA). Our results, consistent with the published in vitro studies, will be useful for the future design of rhenium tricarbonyl diimine-based antibiotics. View Full-Text
Keywords: rhenium; tricarbonyl; antimicrobial; S. aureus; MRSA; AutoDock; membrane; proteins; LspA; LtaA rhenium; tricarbonyl; antimicrobial; S. aureus; MRSA; AutoDock; membrane; proteins; LspA; LtaA
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MDPI and ACS Style

Schindler, K.; Cortat, Y.; Nedyalkova, M.; Crochet, A.; Lattuada, M.; Pavic, A.; Zobi, F. Antimicrobial Activity of Rhenium Di- and Tricarbonyl Diimine Complexes: Insights on Membrane-Bound S. aureus Protein Binding. Pharmaceuticals 2022, 15, 1107. https://doi.org/10.3390/ph15091107

AMA Style

Schindler K, Cortat Y, Nedyalkova M, Crochet A, Lattuada M, Pavic A, Zobi F. Antimicrobial Activity of Rhenium Di- and Tricarbonyl Diimine Complexes: Insights on Membrane-Bound S. aureus Protein Binding. Pharmaceuticals. 2022; 15(9):1107. https://doi.org/10.3390/ph15091107

Chicago/Turabian Style

Schindler, Kevin, Youri Cortat, Miroslava Nedyalkova, Aurelien Crochet, Marco Lattuada, Aleksandar Pavic, and Fabio Zobi. 2022. "Antimicrobial Activity of Rhenium Di- and Tricarbonyl Diimine Complexes: Insights on Membrane-Bound S. aureus Protein Binding" Pharmaceuticals 15, no. 9: 1107. https://doi.org/10.3390/ph15091107

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