Polyoxovanadate inhibition of<i>Escherichia coli</i>growth shows a reverse correlation with Ca<sup>2+</sup>-ATPase inhibition

Marques‐da‐Silva, Dorinda; Fraqueza, Gil; Lagoa, Ricardo; Vannathan, Anjana Anandan; Mal, Sib Sankar; Aureliano, Manuel

doi:10.1039/c9nj01208g

Cited by 33 publications

(20 citation statements)

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“…Ca 2+ -ATPase activities were measured spectrophotometrically (Shimadzu, UV 2401-PC, Shimadzu Corporation, Kyoto, Japan) at 22 • C, using the coupled enzyme pyruvate kinase/lactate dehydrogenase assay, as described elsewhere [21,31,32,34,35]. The reaction medium contained: 25 mM HEPES (pH 7.0), 100 mM KCl, 5 mM MgCl 2 , 50 µM CaCl 2 , and 2.5 mM ATP.…”

Section: Effects Of Gold Compounds In the Atp Hydrolysis By The Sr Camentioning

confidence: 99%

“…Additionally, gold compounds have been a subject of research in terms of antibacterial, antivirus and anti-parasite activity [12,13,16,17] and in Alzheimer's disease [18]. Gold compounds, together with vanadium complexes and polyoxometalates, have been selected by some researchers as alternative anti-tumor substances with promising results in tumor growth suppression [19][20][21][22][23]. Moreover, some of these studies used gold nanoparticles functionalized with polyoxometalates, which are highly uptaken by cancerous cells [13].…”

Section: Introductionmentioning

confidence: 99%

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The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

et al. 2020

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The therapeutic applications of gold are well-known for many centuries. The most used gold compounds contain Au(I). Herein, we report, for the first time, the ability of four Au(I) and Au(III) complexes, namely dichloro (2-pyridinecarboxylate) Au(III) (abbreviated as 1), chlorotrimethylphosphine Au(I) (2), 1,3-bis(2,6-diisopropylphenyl) imidazole-2-ylidene Au(I) chloride (3), and chlorotriphenylphosphine Au(I) (4), to affect the sarcoplasmic reticulum (SR) Ca2+-ATPase activity. The tested gold compounds strongly inhibit the Ca2+-ATPase activity with different effects, being Au(I) compounds 2 and 4 the strongest, with half maximal inhibitory concentration (IC50) values of 0.8 and 0.9 µM, respectively. For Au(III) compound 1 and Au(I) compound 3, higher IC50 values are found (4.5 µM and 16.3 µM, respectively). The type of enzymatic inhibition is also different, with gold compounds 1 and 2 showing a non-competitive inhibition regarding the native substrate MgATP, whereas for Au compounds 3 and 4, a mixed type of inhibition is observed. Our data reveal, for the first time, Au(I) compounds with powerful inhibitory capacity towards SR Ca2+ATPase function. These results also show, unprecedently, that Au (III) and Au(I) compounds can act as P-type ATPase inhibitors, unveiling a potential application of these complexes.

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Section: Effects Of Gold Compounds In the Atp Hydrolysis By The Sr Camentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

et al. 2020

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“…Polyoxometalates (abbreviated as POMs), because of their incomparable structural diversity and novel pharmacological properties, have been widely applied to medicinal chemistry (Bijelic, Aureliano, & Rompel, 2018a, 2018bGao et al, 2014;Li et al, 2019;Marques-da-Silva et al, 2019), especially for enzyme inhibition (Lee et al, 2015;Liu et al, 2016;Stephan, Kubeil, Emmerling, & Müller, 2013). A large number of reports have described that POMs possess potent inhibitory activity of phosphatases, nucleotidases, kinases, sialyltransferases, sulfotransferases, acetylases, nucleases, and proteases (Seko, Yamase, & Yamashita, 2009;Stephan et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Biological evaluation of Keggin‐type polyoxometalates on tyrosinase: Kinetics and molecular modeling

et al. 2020

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Abnormal overexpression of tyrosinase activity can lead to the production of hyperpigmentation in human skin and enzymatic browning in fruits and vegetables. Herein, the inhibition and mechanism of the H3PMo12O40 and two transition metal‐substituted Keggin‐type polyoxometalates (Na7PMo11CoO40 and Na7PMo11ZnO40) on tyrosinase were studied by kinetics and molecular modeling. Kinetic studies indicated that all compounds had more potent inhibitory activities than standard arbutin, and H3PMo12O40 (IC50 = 0.443 ± 0.006 mm) is ~15‐fold stronger inhibition than arbutin. Additionally, all compounds inhibited tyrosinase in a reversible competitive manner. Intriguingly, molecular modeling elucidated that three compounds competitively bind to tyrosinase mainly through more interactions with Cu2+ ions and the amino acid residue capable of forming cation‐π and hydrogen bonding, forming a reversible non‐covalent complex. Molecular simulation study correlated well with the biological activity of three compounds in vitro. This work provided new insights into design and synthesis of polyoxometalates as tyrosinase inhibitors in the field of medicine, cosmetic, and food.

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“…Enzyme inhibition and protein-binding assays with vanadates, mostly with V 1 and V 10 , are generally performed using isolated proteins, mainly ATPases [52]. The use of large POVs and MV-POVs is slowly emerging, but only a few examples are currently available, such as the interaction of phosphotetradecavanadate (PV 14 ) with Na + /K + and Ca 2+ -ATPases [53], and of MnV 11 O 33 5− and MnV 13 O 38 7− with Ca 2+ -ATPase [54]. The inhibition of ATPase activity has also been explored with a variety of polyoxotungstates (POT) [55], as summarized in Table S3.…”

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Polyoxovanadates as new P‐glycoprotein inhibitors: insights into the mechanism of inhibition

et al. 2021

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A promising strategy to overcome multidrug resistance is the use of inhibitors of ABC drug transporters. For this reason, we evaluated the polyoxovanadates (POVs) [V 10 O 28 ] 6-(V 10 ), [H 6 V 14 O 38 (PO 4 )] 5− (V 14 ), [V 15 O 36 Cl] 6− (V 15 ) and [V 18 O 42 I] 7− (V 18 ) as inhibitors of three major multidrug resistance-linked ABC transporters: P-glycoprotein (P-gp), ABCG2 and MRP1. All of the POVs selectively inhibited P-gp. V 10 and V 18 were the two most promising compounds, with IC 50 values of transport inhibition of 25.4 and 22.7 µM, respectively. Both compounds inhibited P-gp ATPase activity, with the same IC 50 value of 1.26 µM. V 10 and V 18 triggered different conformational changes in the P-gp protein with time-dependent inhibition, which was confirmed using the synthesized salt of V 10 with rhodamine B, RhoB-V 10 . The hydrophilic nature of POVs supports the hypothesis that these compounds target an unusual ligand-binding site, opening new possibilities in the development of potent modulators of ABC transporters.

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Polyoxovanadate inhibition ofEscherichia coligrowth shows a reverse correlation with Ca²⁺-ATPase inhibition

Abstract: Polyoxovanadates were recently found to be the most active among a series of polyoxometalates against bacteria. In this study, a reverse correlation was found between the Ca2+-ATPase IC50 and the E. Coli GI50 values.

Cited by 33 publications

References 58 publications

The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

Biological evaluation of Keggin‐type polyoxometalates on tyrosinase: Kinetics and molecular modeling

Polyoxovanadates as new P‐glycoprotein inhibitors: insights into the mechanism of inhibition

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Polyoxovanadate inhibition ofEscherichia coligrowth shows a reverse correlation with Ca2+-ATPase inhibition

Abstract: Polyoxovanadates were recently found to be the most active among a series of polyoxometalates against bacteria. In this study, a reverse correlation was found between the Ca2+-ATPase IC50 and the E. Coli GI50 values.

Cited by 33 publications

References 58 publications

The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

The Ca2+-ATPase Inhibition Potential of Gold(I, III) Compounds

Biological evaluation of Keggin‐type polyoxometalates on tyrosinase: Kinetics and molecular modeling

Polyoxovanadates as new P‐glycoprotein inhibitors: insights into the mechanism of inhibition

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Product

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Polyoxovanadate inhibition ofEscherichia coligrowth shows a reverse correlation with Ca²⁺-ATPase inhibition