TY  - JOUR
AU  - Bondžić, Aleksandra
AU  - Lazarević Pašti, Tamara
AU  - Pasti, Igor
AU  - Bondžić, Bojan
AU  - Momčilović, Miloš D.
AU  - Loosen, Alexandra
AU  - Parac-Vogt Tatjana
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5430
AB  - Organophosphate-based pesticides have remarkably contributed to the agriculture industry, but their toxicity has a large negative impact on the environment as well as on the health of humans and other living organisms. Most of the methods developed to remedy the organophosphate pesticide toxicity are very time-consuming and are based on their adsorption onto different materials and/or their degradation to nontoxic species. In this study, detoxification of three structurally different organophosphate pesticides was investigated using an NU-1000 metal-organic framework. We showed that NU-1000 is an excellent agent for fast (average time ≤ 3 min) and effective removal of organophosphate pesticides with an aromatic heterocyclic moiety. In particular, superior detoxification of chlorpyrifos solution after NU-1000 treatment was achieved after only 1 min. The combination of experimental and computational methods revealed that the synergic effects of sorption and hydrolysis are responsible for the superior removal of CHP by NU-1000. The sorption process occurs on the Zr node (chemisorption) and pyrene linkers (physisorption) following pseudo-first-order kinetics during the first minute, and a pseudo-second-order model fits the entire time range. The multilayer adsorption of chlorpyrifos or its hydrolyzed product, 3,5,6-trichloro-2-pyridinol, takes place on a pyrene linker, whereas the aliphatic part of the molecule remains chemisorbed on the Zr node. Such unique synergy between induced sorption and hydrolysis of chlorpyrifos by NU-1000 results in its fast and effective removal with rapid detoxification in non-buffered solutions.
PB  - USA : American Chemical Society
T2  - ACS Applied Nano Materials
T1  - Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos
VL  - 5
IS  - 3
SP  - 3312
EP  - 3324
DO  - 10.1021/acsanm.1c03863
ER  - 

@article{
author = "Bondžić, Aleksandra and Lazarević Pašti, Tamara and Pasti, Igor and Bondžić, Bojan and Momčilović, Miloš D. and Loosen, Alexandra and Parac-Vogt Tatjana",
year = "2022",
abstract = "Organophosphate-based pesticides have remarkably contributed to the agriculture industry, but their toxicity has a large negative impact on the environment as well as on the health of humans and other living organisms. Most of the methods developed to remedy the organophosphate pesticide toxicity are very time-consuming and are based on their adsorption onto different materials and/or their degradation to nontoxic species. In this study, detoxification of three structurally different organophosphate pesticides was investigated using an NU-1000 metal-organic framework. We showed that NU-1000 is an excellent agent for fast (average time ≤ 3 min) and effective removal of organophosphate pesticides with an aromatic heterocyclic moiety. In particular, superior detoxification of chlorpyrifos solution after NU-1000 treatment was achieved after only 1 min. The combination of experimental and computational methods revealed that the synergic effects of sorption and hydrolysis are responsible for the superior removal of CHP by NU-1000. The sorption process occurs on the Zr node (chemisorption) and pyrene linkers (physisorption) following pseudo-first-order kinetics during the first minute, and a pseudo-second-order model fits the entire time range. The multilayer adsorption of chlorpyrifos or its hydrolyzed product, 3,5,6-trichloro-2-pyridinol, takes place on a pyrene linker, whereas the aliphatic part of the molecule remains chemisorbed on the Zr node. Such unique synergy between induced sorption and hydrolysis of chlorpyrifos by NU-1000 results in its fast and effective removal with rapid detoxification in non-buffered solutions.",
publisher = "USA : American Chemical Society",
journal = "ACS Applied Nano Materials",
title = "Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos",
volume = "5",
number = "3",
pages = "3312-3324",
doi = "10.1021/acsanm.1c03863"
}

Bondžić, A., Lazarević Pašti, T., Pasti, I., Bondžić, B., Momčilović, M. D., Loosen, A.,& Parac-Vogt Tatjana. (2022). Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos. in ACS Applied Nano Materials
USA : American Chemical Society., 5(3), 3312-3324.
https://doi.org/10.1021/acsanm.1c03863

Bondžić A, Lazarević Pašti T, Pasti I, Bondžić B, Momčilović MD, Loosen A, Parac-Vogt Tatjana. Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos. in ACS Applied Nano Materials. 2022;5(3):3312-3324.
doi:10.1021/acsanm.1c03863 .

Bondžić, Aleksandra, Lazarević Pašti, Tamara, Pasti, Igor, Bondžić, Bojan, Momčilović, Miloš D., Loosen, Alexandra, Parac-Vogt Tatjana, "Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos" in ACS Applied Nano Materials, 5, no. 3 (2022):3312-3324,
https://doi.org/10.1021/acsanm.1c03863 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Lazarević-Pašti, Tamara D.
AU  - Leskovac, Andreja R.
AU  - Petrović, Sandra
AU  - Čolović, Mirjana B.
AU  - Parac-Vogt Tatjana
AU  - Janjić, Goran
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3582
AB  - Acetylcholinesterase (AChE) inhibitors are important in the treatment of neurodegenerative diseases. Two inhibitors,
12-tungstosilicic acid (WSiA) and 12-tungstophosphoric acid (WPA), which have polyoxometalate
(POM) type structure, have been shown to inhibit AChE activity in nM concentration. Circular dichroism and
tryptophan fluorescence spectroscopy demonstrated that the AChE inhibition was not accompanied by significant
changes in the secondary structure of the enzyme. The molecular docking approach has revealed a new
allosteric binding site, termed β-allosteric site (β-AS), which is considered responsible for the inhibition of AChE
by POMs. To the best of our knowledge, this is the first study reporting a new allosteric site that is considered
responsible for AChE inhibition by voluminous and negatively charged molecules such as POMs. The selected
POMs were further subjected to genotoxicity testing using human peripheral blood cells as a model system. It
was shown that WSiA and WPA induced a mild cytostatic but not genotoxic effects in human lymphocytes, which
indicates their potential to be used as medicinal drugs. The identification of non-toxic compounds capable of
binding to an allosteric site that so far has not been considered responsible for enzyme inhibition could be
fundamental for the development of new drug design strategies and the discovery of more efficient AChE
modulators.
PB  - Elsevier
T2  - European Journal of Pharmaceutical Sciences
T1  - A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition
VL  - 151
SP  - 105376
DO  - 10.1016/j.ejps.2020.105376
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Lazarević-Pašti, Tamara D. and Leskovac, Andreja R. and Petrović, Sandra and Čolović, Mirjana B. and Parac-Vogt Tatjana and Janjić, Goran",
year = "2020",
abstract = "Acetylcholinesterase (AChE) inhibitors are important in the treatment of neurodegenerative diseases. Two inhibitors,
12-tungstosilicic acid (WSiA) and 12-tungstophosphoric acid (WPA), which have polyoxometalate
(POM) type structure, have been shown to inhibit AChE activity in nM concentration. Circular dichroism and
tryptophan fluorescence spectroscopy demonstrated that the AChE inhibition was not accompanied by significant
changes in the secondary structure of the enzyme. The molecular docking approach has revealed a new
allosteric binding site, termed β-allosteric site (β-AS), which is considered responsible for the inhibition of AChE
by POMs. To the best of our knowledge, this is the first study reporting a new allosteric site that is considered
responsible for AChE inhibition by voluminous and negatively charged molecules such as POMs. The selected
POMs were further subjected to genotoxicity testing using human peripheral blood cells as a model system. It
was shown that WSiA and WPA induced a mild cytostatic but not genotoxic effects in human lymphocytes, which
indicates their potential to be used as medicinal drugs. The identification of non-toxic compounds capable of
binding to an allosteric site that so far has not been considered responsible for enzyme inhibition could be
fundamental for the development of new drug design strategies and the discovery of more efficient AChE
modulators.",
publisher = "Elsevier",
journal = "European Journal of Pharmaceutical Sciences",
title = "A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition",
volume = "151",
pages = "105376",
doi = "10.1016/j.ejps.2020.105376"
}

Bondžić, A. M., Lazarević-Pašti, T. D., Leskovac, A. R., Petrović, S., Čolović, M. B., Parac-Vogt Tatjana,& Janjić, G.. (2020). A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition. in European Journal of Pharmaceutical Sciences
Elsevier., 151, 105376.
https://doi.org/10.1016/j.ejps.2020.105376

Bondžić AM, Lazarević-Pašti TD, Leskovac AR, Petrović S, Čolović MB, Parac-Vogt Tatjana, Janjić G. A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition. in European Journal of Pharmaceutical Sciences. 2020;151:105376.
doi:10.1016/j.ejps.2020.105376 .

Bondžić, Aleksandra M., Lazarević-Pašti, Tamara D., Leskovac, Andreja R., Petrović, Sandra, Čolović, Mirjana B., Parac-Vogt Tatjana, Janjić, Goran, "A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition" in European Journal of Pharmaceutical Sciences, 151 (2020):105376,
https://doi.org/10.1016/j.ejps.2020.105376 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Janjić, Goran
AU  - Dramićanin, Miroslav
AU  - Messori, Luigi
AU  - Massai, Lara
AU  - Parac-Vogt Tatjana
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2179
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.
PB  - Royal Soc Chemistry, Cambridge
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 and Dramićanin, Miroslav and Messori, Luigi and Massai, Lara and Parac-Vogt Tatjana 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.",
publisher = "Royal Soc Chemistry, Cambridge",
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., Dramićanin, M., Messori, L., Massai, L., Parac-Vogt Tatjana,& 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
Royal Soc Chemistry, Cambridge., 9(3), 292-300.
https://doi.org/10.1039/c7mt00017k

Bondžić AM, Janjić G, Dramićanin M, Messori L, Massai L, Parac-Vogt Tatjana, 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, Dramićanin, Miroslav, Messori, Luigi, Massai, Lara, Parac-Vogt Tatjana, 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 . .