TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Leskovac, Andreja
AU  - Petrović, Sandra
AU  - Vasić Anićijević, Dragana D.
AU  - Luce, Marco
AU  - Massai, Lara
AU  - Generosi, Amanda
AU  - Paci, Barbara
AU  - Cricenti, Antonio
AU  - Messori, Luigi
AU  - Vasić, Vesna M.
PY  - 2019
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8747
AB  - Citrate-capped gold nanoparticles (AuNPs) were functionalized with three distinct antitumor gold(III) complexes, e.g., [Au(N,N)(OH)2][PF6], where (N,N)=2,2′-bipyridine; [Au(C,N)(AcO)2], where (C,N)=deprotonated 6-(1,1-dimethylbenzyl)-pyridine; [Au(C,N,N)(OH)][PF6], where (C,N,N)=deprotonated 6-(1,1-dimethylbenzyl)-2,2′-bipyridine, to assess the chance of tracking their subcellular distribution by atomic force microscopy (AFM), and surface enhanced Raman spectroscopy (SERS) techniques. An extensive physicochemical characterization of the formed conjugates was, thus, carried out by applying a variety of methods (density functional theory—DFT, UV/Vis spectrophotometry, AFM, Raman spectroscopy, and SERS). The resulting gold(III) complexes/AuNPs conjugates turned out to be pretty stable. Interestingly, they exhibited a dramatically increased resonance intensity in the Raman spectra induced by AuNPs. For testing the use of the functionalized AuNPs for biosensing, their distribution in the nuclear, cytosolic, and membrane cell fractions obtained from human lymphocytes was investigated by AFM and SERS. The conjugates were detected in the membrane and nuclear cell fractions but not in the cytosol. The AFM method confirmed that conjugates induced changes in the morphology and nanostructure of the membrane and nuclear fractions. The obtained results point out that the conjugates formed between AuNPs and gold(III) complexes may be used as a tool for tracking metallodrug distribution in the different cell fractions.
T2  - International Journal of Molecular Sciences
T1  - Conjugates of Gold Nanoparticles and Antitumor Gold(III) Complexes as a Tool for Their AFM and SERS Detection in Biological Tissue
VL  - 20
IS  - 24
SP  - 6306
DO  - 10.3390/ijms20246306
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Leskovac, Andreja and Petrović, Sandra and Vasić Anićijević, Dragana D. and Luce, Marco and Massai, Lara and Generosi, Amanda and Paci, Barbara and Cricenti, Antonio and Messori, Luigi and Vasić, Vesna M.",
year = "2019",
abstract = "Citrate-capped gold nanoparticles (AuNPs) were functionalized with three distinct antitumor gold(III) complexes, e.g., [Au(N,N)(OH)2][PF6], where (N,N)=2,2′-bipyridine; [Au(C,N)(AcO)2], where (C,N)=deprotonated 6-(1,1-dimethylbenzyl)-pyridine; [Au(C,N,N)(OH)][PF6], where (C,N,N)=deprotonated 6-(1,1-dimethylbenzyl)-2,2′-bipyridine, to assess the chance of tracking their subcellular distribution by atomic force microscopy (AFM), and surface enhanced Raman spectroscopy (SERS) techniques. An extensive physicochemical characterization of the formed conjugates was, thus, carried out by applying a variety of methods (density functional theory—DFT, UV/Vis spectrophotometry, AFM, Raman spectroscopy, and SERS). The resulting gold(III) complexes/AuNPs conjugates turned out to be pretty stable. Interestingly, they exhibited a dramatically increased resonance intensity in the Raman spectra induced by AuNPs. For testing the use of the functionalized AuNPs for biosensing, their distribution in the nuclear, cytosolic, and membrane cell fractions obtained from human lymphocytes was investigated by AFM and SERS. The conjugates were detected in the membrane and nuclear cell fractions but not in the cytosol. The AFM method confirmed that conjugates induced changes in the morphology and nanostructure of the membrane and nuclear fractions. The obtained results point out that the conjugates formed between AuNPs and gold(III) complexes may be used as a tool for tracking metallodrug distribution in the different cell fractions.",
journal = "International Journal of Molecular Sciences",
title = "Conjugates of Gold Nanoparticles and Antitumor Gold(III) Complexes as a Tool for Their AFM and SERS Detection in Biological Tissue",
volume = "20",
number = "24",
pages = "6306",
doi = "10.3390/ijms20246306"
}

Bondžić, A. M., Leskovac, A., Petrović, S., Vasić Anićijević, D. D., Luce, M., Massai, L., Generosi, A., Paci, B., Cricenti, A., Messori, L.,& Vasić, V. M.. (2019). Conjugates of Gold Nanoparticles and Antitumor Gold(III) Complexes as a Tool for Their AFM and SERS Detection in Biological Tissue. in International Journal of Molecular Sciences, 20(24), 6306.
https://doi.org/10.3390/ijms20246306

Bondžić AM, Leskovac A, Petrović S, Vasić Anićijević DD, Luce M, Massai L, Generosi A, Paci B, Cricenti A, Messori L, Vasić VM. Conjugates of Gold Nanoparticles and Antitumor Gold(III) Complexes as a Tool for Their AFM and SERS Detection in Biological Tissue. in International Journal of Molecular Sciences. 2019;20(24):6306.
doi:10.3390/ijms20246306 .

Bondžić, Aleksandra M., Leskovac, Andreja, Petrović, Sandra, Vasić Anićijević, Dragana D., Luce, Marco, Massai, Lara, Generosi, Amanda, Paci, Barbara, Cricenti, Antonio, Messori, Luigi, Vasić, Vesna M., "Conjugates of Gold Nanoparticles and Antitumor Gold(III) Complexes as a Tool for Their AFM and SERS Detection in Biological Tissue" in International Journal of Molecular Sciences, 20, no. 24 (2019):6306,
https://doi.org/10.3390/ijms20246306 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Čolović, Mirjana B.
AU  - Janjić, Goran V.
AU  - Zarić, Božidarka
AU  - Petrović, Sandra
AU  - Krstić, Danijela Z.
AU  - Marzo, Tiziano
AU  - Messori, Luigi
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1648
AB  - The in vitro effects of oxo-bridged binuclear gold(III) complexes, i.e., [(bipy2Me)(2)Au-2(mu-O)(2)][PF6](2) (Auoxo6), Au-2[(bipydmb-H)(2)(mu-O)][PF6] (Au(2)bipyC) and [Au-2(phen(2Me))(2)(mu-O)(2)](PF6)(2) (Au(2)phen) on Na/K-ATPase, purified from the porcine cerebral cortex, were investigated. All three studied gold complexes inhibited the enzyme activity in a concentration-dependent manner achieving IC50 values in the low micromolar range. Kinetic analysis suggested an uncompetitive mode of inhibition for Auoxo6 and Au(2)bipyC, and a mixed type one for Au(2)phen. Docking studies indicated that the inhibitory actions of all tested complexes are related to E2-P enzyme conformation binding to ion channel and intracellular part between N and P sub-domain. In addition, Au(2)phen was able to inhibit the enzyme by interacting with its extracellular part as well. Toxic effects of the gold(III) complexes were evaluated in vitro by following lactate dehydrogenase activity in rat brain synaptosomes and incidence of micronuclei and cytokinesis-block proliferation index in cultivated human lymphocytes. All investigated complexes turned out to induce cytogenetic damage consisting of a significant decrease in cell proliferation and an increase in micronuclei in a dose-dependent manner. On the other hand, lactate dehydrogenase activity, an indicator of membrane integrity/viability, was not affected by Auoxo6 and Au(2)bipyC, while Au(2)phen slightly modified its activity.
T2  - Journal of Biological Inorganic Chemistry
T1  - The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach
VL  - 22
IS  - 6
SP  - 819
EP  - 832
DO  - 10.1007/s00775-017-1460-5
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Čolović, Mirjana B. and Janjić, Goran V. and Zarić, Božidarka and Petrović, Sandra and Krstić, Danijela Z. and Marzo, Tiziano and Messori, Luigi and Vasić, Vesna M.",
year = "2017",
abstract = "The in vitro effects of oxo-bridged binuclear gold(III) complexes, i.e., [(bipy2Me)(2)Au-2(mu-O)(2)][PF6](2) (Auoxo6), Au-2[(bipydmb-H)(2)(mu-O)][PF6] (Au(2)bipyC) and [Au-2(phen(2Me))(2)(mu-O)(2)](PF6)(2) (Au(2)phen) on Na/K-ATPase, purified from the porcine cerebral cortex, were investigated. All three studied gold complexes inhibited the enzyme activity in a concentration-dependent manner achieving IC50 values in the low micromolar range. Kinetic analysis suggested an uncompetitive mode of inhibition for Auoxo6 and Au(2)bipyC, and a mixed type one for Au(2)phen. Docking studies indicated that the inhibitory actions of all tested complexes are related to E2-P enzyme conformation binding to ion channel and intracellular part between N and P sub-domain. In addition, Au(2)phen was able to inhibit the enzyme by interacting with its extracellular part as well. Toxic effects of the gold(III) complexes were evaluated in vitro by following lactate dehydrogenase activity in rat brain synaptosomes and incidence of micronuclei and cytokinesis-block proliferation index in cultivated human lymphocytes. All investigated complexes turned out to induce cytogenetic damage consisting of a significant decrease in cell proliferation and an increase in micronuclei in a dose-dependent manner. On the other hand, lactate dehydrogenase activity, an indicator of membrane integrity/viability, was not affected by Auoxo6 and Au(2)bipyC, while Au(2)phen slightly modified its activity.",
journal = "Journal of Biological Inorganic Chemistry",
title = "The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach",
volume = "22",
number = "6",
pages = "819-832",
doi = "10.1007/s00775-017-1460-5"
}

Bondžić, A. M., Čolović, M. B., Janjić, G. V., Zarić, B., Petrović, S., Krstić, D. Z., Marzo, T., Messori, L.,& Vasić, V. M.. (2017). The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach. in Journal of Biological Inorganic Chemistry, 22(6), 819-832.
https://doi.org/10.1007/s00775-017-1460-5

Bondžić AM, Čolović MB, Janjić GV, Zarić B, Petrović S, Krstić DZ, Marzo T, Messori L, Vasić VM. The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach. in Journal of Biological Inorganic Chemistry. 2017;22(6):819-832.
doi:10.1007/s00775-017-1460-5 .

Bondžić, Aleksandra M., Čolović, Mirjana B., Janjić, Goran V., Zarić, Božidarka, Petrović, Sandra, Krstić, Danijela Z., Marzo, Tiziano, Messori, Luigi, Vasić, Vesna M., "The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach" in Journal of Biological Inorganic Chemistry, 22, no. 6 (2017):819-832,
https://doi.org/10.1007/s00775-017-1460-5 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Janjić, Goran V.
AU  - Dramićanin, Miroslav
AU  - Messori, Luigi
AU  - Massai, Lara
AU  - Parac-Vogt, Tatjana N.
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1476
AB  - Na/K-ATPase is emerging as an important target for a variety of anticancer metal-based drugs. The interactions of Na/K-ATPase (in its E1 state) with three representative and structurally related cytotoxic gold(III) complexes, i.e. [Au(bipy)(OH)(2)][PF6], bipy = 2,2-bipyridine; [Au(py(dmb)-H)(CH3COO)(2)], py(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-pyridine and [Au(bipy(dmb)-H)(OH)][PF6], bipy(c)-H = deprotonated 6-(1,1-dimethylbenzyl)-2,20-bipyridine, are investigated here in depth using a variety of spectroscopic methods, in combination with docking studies. Detailed information is gained on the conformational and structural changes experienced by the enzyme upon binding of these gold(III) complexes. The quenching constants of intrinsic enzyme fluorescence, the fraction of Trp residues accessible to gold(III) complexes and the reaction stoichiometries were determined in various cases. Specific hypotheses are made concerning the binding mode of these gold(III) complexes to the enzyme and the likely binding sites. Differences in their binding behaviour toward Na/K-ATPase are explained on the ground of their distinctive structural features. The present results offer further support to the view that Na/K-ATPase may be a relevant biomolecular target for cytotoxic gold(III) compounds of medicinal interest and may thus be involved in their overall mode of action.
T2  - Metallomics
T1  - Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes
VL  - 9
IS  - 3
SP  - 292
EP  - 300
DO  - 10.1039/c7mt00017k
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Janjić, Goran V. and Dramićanin, Miroslav and Messori, Luigi and Massai, Lara and Parac-Vogt, Tatjana N. and Vasić, Vesna M.",
year = "2017",
abstract = "Na/K-ATPase is emerging as an important target for a variety of anticancer metal-based drugs. The interactions of Na/K-ATPase (in its E1 state) with three representative and structurally related cytotoxic gold(III) complexes, i.e. [Au(bipy)(OH)(2)][PF6], bipy = 2,2-bipyridine; [Au(py(dmb)-H)(CH3COO)(2)], py(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-pyridine and [Au(bipy(dmb)-H)(OH)][PF6], bipy(c)-H = deprotonated 6-(1,1-dimethylbenzyl)-2,20-bipyridine, are investigated here in depth using a variety of spectroscopic methods, in combination with docking studies. Detailed information is gained on the conformational and structural changes experienced by the enzyme upon binding of these gold(III) complexes. The quenching constants of intrinsic enzyme fluorescence, the fraction of Trp residues accessible to gold(III) complexes and the reaction stoichiometries were determined in various cases. Specific hypotheses are made concerning the binding mode of these gold(III) complexes to the enzyme and the likely binding sites. Differences in their binding behaviour toward Na/K-ATPase are explained on the ground of their distinctive structural features. The present results offer further support to the view that Na/K-ATPase may be a relevant biomolecular target for cytotoxic gold(III) compounds of medicinal interest and may thus be involved in their overall mode of action.",
journal = "Metallomics",
title = "Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes",
volume = "9",
number = "3",
pages = "292-300",
doi = "10.1039/c7mt00017k"
}

Bondžić, A. M., Janjić, G. V., Dramićanin, M., Messori, L., Massai, L., Parac-Vogt, T. N.,& Vasić, V. M.. (2017). Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes. in Metallomics, 9(3), 292-300.
https://doi.org/10.1039/c7mt00017k

Bondžić AM, Janjić GV, Dramićanin M, Messori L, Massai L, Parac-Vogt TN, Vasić VM. Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes. in Metallomics. 2017;9(3):292-300.
doi:10.1039/c7mt00017k .

Bondžić, Aleksandra M., Janjić, Goran V., Dramićanin, Miroslav, Messori, Luigi, Massai, Lara, Parac-Vogt, Tatjana N., Vasić, Vesna M., "Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes" in Metallomics, 9, no. 3 (2017):292-300,
https://doi.org/10.1039/c7mt00017k . .

TY  - JOUR
AU  - Petrović, Voin
AU  - Petrović, Sandra
AU  - Joksić, Gordana
AU  - Savić, Jasmina
AU  - Čolović, Mirjana B.
AU  - Cinellu, Maria Agostina
AU  - Massai, Lara
AU  - Messori, Luigi
AU  - Vasić, Vesna M.
PY  - 2014
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/140
AB  - Na+/K+-ATPase is in charge of maintaining the ionic and osmotic intracellular balance by using ATP as an energy source to drive excess Na+ ions out of the cell in exchange for K+ ions. We explored whether three representative cytotoxic gold(III) compounds might interfere with Na+/K+-ATPase and cause its inhibition at pharmacologically relevant concentrations. The tested complexes were [Au(bipy)(OH)(2)][PF6] (bipy = 2,2-bipyridine), [Au (py(dmb)-H)(CH3COO)(2)] (py(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-pyridine), and [Au(bipy(dmb)-H)(OH)][PF6] (bipy(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-2,2-bipyridine). We found that all of them caused a pronounced and similar inhibition of Na+/K+-ATPase activity. Inhibition was found to be non-competitive and reversible. Remarkably, treatment with cysteine resulted in reversal or prevention of Na+/K+-ATPase inhibition. It is very likely that the described effects may contribute to the overall cytotoxic profile of these gold complexes. (C) 2014 Elsevier Inc. All rights reserved.
T2  - Journal of Inorganic Biochemistry
T1  - Inhibition of Na+/K+-ATPase and cytotoxicity of a few selected gold(III) complexes
VL  - 140
SP  - 228
EP  - 235
DO  - 10.1016/j.jinorgbio.2014.07.015
ER  - 

@article{
author = "Petrović, Voin and Petrović, Sandra and Joksić, Gordana and Savić, Jasmina and Čolović, Mirjana B. and Cinellu, Maria Agostina and Massai, Lara and Messori, Luigi and Vasić, Vesna M.",
year = "2014",
abstract = "Na+/K+-ATPase is in charge of maintaining the ionic and osmotic intracellular balance by using ATP as an energy source to drive excess Na+ ions out of the cell in exchange for K+ ions. We explored whether three representative cytotoxic gold(III) compounds might interfere with Na+/K+-ATPase and cause its inhibition at pharmacologically relevant concentrations. The tested complexes were [Au(bipy)(OH)(2)][PF6] (bipy = 2,2-bipyridine), [Au (py(dmb)-H)(CH3COO)(2)] (py(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-pyridine), and [Au(bipy(dmb)-H)(OH)][PF6] (bipy(dmb)-H = deprotonated 6-(1,1-dimethylbenzyl)-2,2-bipyridine). We found that all of them caused a pronounced and similar inhibition of Na+/K+-ATPase activity. Inhibition was found to be non-competitive and reversible. Remarkably, treatment with cysteine resulted in reversal or prevention of Na+/K+-ATPase inhibition. It is very likely that the described effects may contribute to the overall cytotoxic profile of these gold complexes. (C) 2014 Elsevier Inc. All rights reserved.",
journal = "Journal of Inorganic Biochemistry",
title = "Inhibition of Na+/K+-ATPase and cytotoxicity of a few selected gold(III) complexes",
volume = "140",
pages = "228-235",
doi = "10.1016/j.jinorgbio.2014.07.015"
}

Petrović, V., Petrović, S., Joksić, G., Savić, J., Čolović, M. B., Cinellu, M. A., Massai, L., Messori, L.,& Vasić, V. M.. (2014). Inhibition of Na+/K+-ATPase and cytotoxicity of a few selected gold(III) complexes. in Journal of Inorganic Biochemistry, 140, 228-235.
https://doi.org/10.1016/j.jinorgbio.2014.07.015

Petrović V, Petrović S, Joksić G, Savić J, Čolović MB, Cinellu MA, Massai L, Messori L, Vasić VM. Inhibition of Na+/K+-ATPase and cytotoxicity of a few selected gold(III) complexes. in Journal of Inorganic Biochemistry. 2014;140:228-235.
doi:10.1016/j.jinorgbio.2014.07.015 .

Petrović, Voin, Petrović, Sandra, Joksić, Gordana, Savić, Jasmina, Čolović, Mirjana B., Cinellu, Maria Agostina, Massai, Lara, Messori, Luigi, Vasić, Vesna M., "Inhibition of Na+/K+-ATPase and cytotoxicity of a few selected gold(III) complexes" in Journal of Inorganic Biochemistry, 140 (2014):228-235,
https://doi.org/10.1016/j.jinorgbio.2014.07.015 . .