Parac Vogt, Tatjana N.

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  • Parac Vogt, Tatjana N. (2)

Author's Bibliography

A new acetylcholinesterase allosteric site responsible for binding voluminous negatively charged molecules – the role in the mechanism of AChE inhibition

Bondžić, Aleksandra M.; Lazarević-Pašti, Tamara; Leskovac, Andreja; Petrović, Sandra; Čolović, Mirjana B.; Parac Vogt, Tatjana N.; Janjić, Goran V.

(2020)

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Lazarević-Pašti, Tamara
AU  - Leskovac, Andreja
AU  - Petrović, Sandra
AU  - Čolović, Mirjana B.
AU  - Parac Vogt, Tatjana N.
AU  - Janjić, Goran V.
PY  - 2020
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9028
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 andtryptophan fluorescence spectroscopy demonstrated that the AChE inhibition was not accompanied by significantchanges in the secondary structure of the enzyme. The molecular docking approach has revealed a newallosteric binding site, termed β-allosteric site (β-AS), which is considered responsible for the inhibition of AChEby POMs. To the best of our knowledge, this is the first study reporting a new allosteric site that is consideredresponsible for AChE inhibition by voluminous and negatively charged molecules such as POMs. The selectedPOMs were further subjected to genotoxicity testing using human peripheral blood cells as a model system. Itwas shown that WSiA and WPA induced a mild cytostatic but not genotoxic effects in human lymphocytes, whichindicates their potential to be used as medicinal drugs. The identification of non-toxic compounds capable ofbinding to an allosteric site that so far has not been considered responsible for enzyme inhibition could befundamental for the development of new drug design strategies and the discovery of more efficient AChEmodulators.
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 and Leskovac, Andreja and Petrović, Sandra and Čolović, Mirjana B. and Parac Vogt, Tatjana N. and Janjić, Goran V.",
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 andtryptophan fluorescence spectroscopy demonstrated that the AChE inhibition was not accompanied by significantchanges in the secondary structure of the enzyme. The molecular docking approach has revealed a newallosteric binding site, termed β-allosteric site (β-AS), which is considered responsible for the inhibition of AChEby POMs. To the best of our knowledge, this is the first study reporting a new allosteric site that is consideredresponsible for AChE inhibition by voluminous and negatively charged molecules such as POMs. The selectedPOMs were further subjected to genotoxicity testing using human peripheral blood cells as a model system. Itwas shown that WSiA and WPA induced a mild cytostatic but not genotoxic effects in human lymphocytes, whichindicates their potential to be used as medicinal drugs. The identification of non-toxic compounds capable ofbinding to an allosteric site that so far has not been considered responsible for enzyme inhibition could befundamental for the development of new drug design strategies and the discovery of more efficient AChEmodulators.",
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., Leskovac, A., Petrović, S., Čolović, M. B., Parac Vogt, T. N.,& Janjić, G. V.. (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, 151, 105376.
https://doi.org/10.1016/j.ejps.2020.105376
Bondžić AM, Lazarević-Pašti T, Leskovac A, Petrović S, Čolović MB, Parac Vogt TN, Janjić GV. 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, Leskovac, Andreja, Petrović, Sandra, Čolović, Mirjana B., Parac Vogt, Tatjana N., Janjić, Goran V., "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 . .
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Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes

Bondžić, Aleksandra M.; Janjić, Goran V.; Dramićanin, Miroslav; Messori, Luigi; Massai, Lara; Parac Vogt, Tatjana N.; Vasić, Vesna M.

(2017)

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 . .
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