Impact of Cu2+ ions on the structure of colistin and cell-free system nucleic acid degradation

Stokowa-Sołtys, Kamila; Kasprowicz, Aleksandra; Wrzesiński, Jan; Ciesiołka, Jerzy; Gaggelli, Nicola; Gaggelli, Elena; Valensin, Gianni; Jeżowska‐Bojczuk, Małgorzata

doi:10.1016/j.jinorgbio.2015.05.011

Cited by 10 publications

(10 citation statements)

References 56 publications

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“…The significant change in the mutual position of hydrophilic and hydrophobic groups of amphisin was observed after ion binding. In accordance with previous findings [42], three amide nitrogens can coordinate Cu 2+ ion in planar configurations. Additionally, in this complex the oxygen atom from the side chain of the Asp amino acid is directly involved in metal ion binding (Fig.…”

Section: Amphisinsupporting

confidence: 93%

See 1 more Smart Citation

Study of metal-lipopeptide complexes and their self-assembly behavior, micelle formation, interaction with bovine serum albumin and biological properties

Janek

Rodrigues

Czyżnikowska

2018

Journal of Molecular Liquids

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The present study aimed to explore the interactions of divalent counterions with biomolecular amphisin using circular dichroism (CD), ultraviolet-visible (UV-Vis) and density functional theory (DFT). The binding mode of interactions between metal-amphisin complexes and bovine serum albumin (BSA) were studied using fluorescence spectroscopy. The results showed that Cu 2+ is coordinated by one oxygen atom of the aspartic acid side chain and three amide nitrogen atoms, whereas Zn 2+ , Ca 2+ and Mg 2+ favour the association with backbone oxygen atoms of the amphisin. On the other hand, the aggregation of amphisin induced by divalent counterions was studied by dynamic light scattering (DLS). Our results revealed that the self-assembly process of amphisin can be controlled by the addition of metal ions. The results of CD spectra demonstrated that the binding of divalent counterions to the lipopeptide induces conformational changes in amphisin. Further studies using fluorescence spectroscopy showed that the metal-lipopeptide systems could interact with some functional groups of BSA, increasing the microenvironment around Trp residues of BSA. Thus, the interaction data acquired herein for the interesting class of complexes will be of significance in metal-based drug discovery and developmental research.

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Section: Amphisinsupporting

confidence: 93%

“…Cu in to consideration the results of previous research on the impact of Cu 2+ , Zn 2+, Mg 2+ and Ca 2+ on the binding properties of lipopeptides and cyclic peptides [21,42,43]. It should be underlined that for most analyzed conformation we obtained stable lipopeptide-metal complexes what supports our experimental results.…”

Section: Amphisinsupporting

confidence: 87%

Study of metal-lipopeptide complexes and their self-assembly behavior, micelle formation, interaction with bovine serum albumin and biological properties

Janek

Rodrigues

Czyżnikowska

2018

Journal of Molecular Liquids

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“…Our findings suggest that the structural parameters are highly dependent on the metal binding site. In both conformations presented below, copper is coordinated by three nitrogens, which is in good agreement with previous findings [16]. According to that study, amino and two amide groups of colistin were suggested to be involved in the copper ion binding [16].…”

Section: Molecular Modelling Simulationsupporting

confidence: 91%

“…The Cterminal carboxylic group of the last amino acid forms a lactone with the hydroxyl of Thr3 [3]. One of the most advantageous property that has been reported for pseudofactin II is its ability to inhibit the bacterial adhesion (the first stage of biofilm formation) of Escherichia coli, Enterococcus faecalis, Enterococcus hirae, Staphylococcus epidermidis, Proteus mirabilis, as well as the adhesion of occurring cyclic peptides and lipopeptides such as colistin [14][15][16], polymyxin B [17] and daptomycin [18,19] are known to bind ions and mediate their transport across natural and prepared biological membranes.…”

Section: Introductionmentioning

confidence: 99%

Structure and mode of action of cyclic lipopeptide pseudofactin II with divalent metal ions

Janek

Rodrigues

Gudiña

et al. 2016

Colloids and Surfaces B: Biointerfaces

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The interaction of natural lipopeptide pseudofactin II with a series of doubly charged metal cations was examined by matrix-assisted laser-desorption ionization-time of flight (MALDI-TOF) mass spectrometry and molecular modelling. The molecular modelling for metal-pseudofactin II provides information on the metal-peptide binding sites. Overall, Mg(2+), Ca(2+) and Zn(2+) favor the association with oxygen atoms spanning the peptide backbone, whereas Cu(2+) is coordinated by three nitrogens. Circular dichroism (CD) results confirmed that Zn(2+) and Cu(2+) can disrupt the secondary structure of pseudofactin II at high concentrations, while Ca(2+) and Mg(2+) did not essentially affect the structure of the lipopeptide. Interestingly, our results showed that the addition of Zn(2+) and Cu(2+) helped smaller micelles to form larger micellar aggregates. Since pseudofactin II binds metals, we tested whether this phenomena was somehow related to its antimicrobial activity against Staphylococcus epidermidis and Proteus mirabilis. We found that the antimicrobial effect of pseudofactin II was increased by supplementation of culture media with all tested divalent metal ions. Finally, by using Gram-positive and Gram-negative bacteria we showed that the higher antimicrobial activity of metal complexes of pseudofactin II is attributed to the disruption of the cytoplasmic membrane.

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“…This value corresponds to the removal of a proton from the second amide group and suggests its involvement in the coordination process. 42 This is supported by the spectroscopic data analysis. Spectral parameters are characteristic for the system with three nitrogen donors bound to the Cu(II) ion.…”

Section: Investigation Of Cu(ii) Binding By Viomycinsupporting

confidence: 55%

Studies of viomycin, an anti-tuberculosis antibiotic: copper(ii) coordination, DNA degradation and the impact on delta ribozyme cleavage activity

et al. 2016

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Viomycin is a basic peptide antibiotic, which is among the most effective agents against multidrug-resistant tuberculosis. In this paper we provide the characteristics of its acid base properties, coordination preferences towards the Cu(ii) ions, as well as the reactivity of the resulting complexes against plasmid DNA and HDV ribozyme. Careful coordination studies throughout the wide pH range allow for the characterisation of all the Cu(ii)-viomycin complex species. The assignment of proton chemical shifts was achieved by NMR experiments, while the DTF level of theory was applied to support molecular structures of the studied complexes. The experiments with the plasmid DNA reveal that at the physiological levels of hydrogen peroxide the Cu(ii)-viomycin complex is more aggressive against DNA than uncomplexed metal ions. Moreover, the degradation of DNA by viomycin can be carried out without the presence of transition metal ions. In the studies of antigenomic delta ribozyme catalytic activity, viomycin and its complex are shown to modulate the ribozyme functioning. The molecular modelling approach allows the indication of two different locations of viomycin binding sites to the ribozyme.

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Impact of Cu2+ ions on the structure of colistin and cell-free system nucleic acid degradation

Cited by 10 publications

References 56 publications

Study of metal-lipopeptide complexes and their self-assembly behavior, micelle formation, interaction with bovine serum albumin and biological properties

Study of metal-lipopeptide complexes and their self-assembly behavior, micelle formation, interaction with bovine serum albumin and biological properties

Structure and mode of action of cyclic lipopeptide pseudofactin II with divalent metal ions

Studies of viomycin, an anti-tuberculosis antibiotic: copper(ii) coordination, DNA degradation and the impact on delta ribozyme cleavage activity

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