Janjić, Goran V.

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Authority KeyName Variants
orcid::0000-0002-4138-2637
  • Janjić, Goran V. (12)
Projects
Studies of enzyme interactions with toxic and pharmacologically active molecules Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200017 (University of Belgrade, Institute of Nuclear Sciences 'Vinča', Belgrade-Vinča)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200026 (University of Belgrade, Institute of Chemistry, Technology and Metallurgy - IChTM) Study of structure-function relationships in the plant cell wall and modifications of the wall structure by enzyme engineering
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200135 (University of Belgrade, Faculty of Technology and Metallurgy) Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200146 (University of Belgrade, Faculty of Physical Chemistry)
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200162 (University of Belgrade, Faculty of Physics) Advanced technologies for monitoring and environmental protection from chemical pollutants and radiation burden
Beneficentia Stiftung (Vaduz), ITT (Istituto Toscano Tumori), Fondazione Cassa Risparmio Firenze (CRF), AIRC [IG-16049], AIRC-FIRC (Fondazione Italiana per la Ricerca sul Cancro) [18044] Beneficentia Stiftung (Vaduz, Liechtenstein), AIRC [IG-16049], ITT, Fondazione CRF, CIRCMSB
CCDR-N [NORTE-01-0145-FEDER-000019] CMST COST Action [CM1203 (PoCheMoN)]
COST action CM1203 Polyoxometalate Chemistry for Molecular Nanoscience (PoCheMoN), COST-STSM-ECOST-STSM-CM1203-030416-072554 COST Action [MP1302]
European Union (EU) [600375] Humboldt Foundation
Impact of agents with potential use in functional foods on biomarkers for induction of age related diseases Mechanistic studies of the reactions of transition metal ion complexes with biologically relevant molecules
Noncovalent interactions of pi-systems and their role in molecular recognition info:eu-repo/grantAgreement/MESTD/inst-2020/200026/RS/
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200122 (University of Kragujevac, Faculty of Science) Synthesis of nanopowders and processing of ceramics and nanocomposites with specific electric and magnetic properties for application in integrated passive components

Author's Bibliography

Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action

Bondžić, Aleksandra M.; Žakula, Jelena J.; Korićanac, Lela B.; Keta, Otilija D.; Janjić, Goran V.; Đorđević, Ivana S.; Rajković, Snežana U.

(2021)

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Žakula, Jelena J.
AU  - Korićanac, Lela B.
AU  - Keta, Otilija D.
AU  - Janjić, Goran V.
AU  - Đorđević, Ivana S.
AU  - Rajković, Snežana U.
PY  - 2021
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10015
AB  - Herein, the stability, lipophilicity, in vitro cytotoxicity, and influence on acetylcholinesterase of five dinuclear platinum(II) complexes with the general formula [{Pt(en)Cl}2(μ-L)]2+ (L is a different aromatic nitrogen-containing heterocyclic bridging ligands pyrazine (pz, Pt1), pyridazine (pydz, Pt2), quinoxaline (qx, Pt3), phthalazine (phtz, Pt4) and quinazoline (qz, Pt5), while en is bidentate coordinated ethylenediamine) were evaluated. The most active analyzed platinum complexes induced time-dependent growth inhibition of A375, HeLa, PANC-1, and MRC-5 cells. The best efficiency was achieved on HeLa and PANC-1 cells for Pt1, Pt2, and Pt3 at the highest concentration, while Pt1 was significantly more potent than cisplatin at a lower concentration. Additionally, a lower effect on normal cells was observed compared to cisplatin, which may indicate potentially fewer side effects of these complexes. Selected complexes induce reactive oxygen species and apoptosis on tumor cell lines. The most potent reversible acetylcholinesterase (AChE) inhibitors were Pt2, Pt4, and Pt5. Pt1 showed similar inhibitory potential toward AChE as cisplatin, but a different type of inhibition, which could contribute to lower neurotoxicity. Docking studies revealed that Pt2 and Pt4 were bound to the active gorge above the catalytic triad. In contrast, the other complexes were bound to the edge of the active gorge without impeding the approach to the catalytic triad. According to this, Pt1 represents a promising compound with potent anticancer properties, high selectivity, and low neurotoxicity.
T2  - Chemico-Biological Interactions
T1  - Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action
SP  - 109708
DO  - 10.1016/j.cbi.2021.109708
ER  - 
@article{
author = "Bondžić, Aleksandra M. and Žakula, Jelena J. and Korićanac, Lela B. and Keta, Otilija D. and Janjić, Goran V. and Đorđević, Ivana S. and Rajković, Snežana U.",
year = "2021",
abstract = "Herein, the stability, lipophilicity, in vitro cytotoxicity, and influence on acetylcholinesterase of five dinuclear platinum(II) complexes with the general formula [{Pt(en)Cl}2(μ-L)]2+ (L is a different aromatic nitrogen-containing heterocyclic bridging ligands pyrazine (pz, Pt1), pyridazine (pydz, Pt2), quinoxaline (qx, Pt3), phthalazine (phtz, Pt4) and quinazoline (qz, Pt5), while en is bidentate coordinated ethylenediamine) were evaluated. The most active analyzed platinum complexes induced time-dependent growth inhibition of A375, HeLa, PANC-1, and MRC-5 cells. The best efficiency was achieved on HeLa and PANC-1 cells for Pt1, Pt2, and Pt3 at the highest concentration, while Pt1 was significantly more potent than cisplatin at a lower concentration. Additionally, a lower effect on normal cells was observed compared to cisplatin, which may indicate potentially fewer side effects of these complexes. Selected complexes induce reactive oxygen species and apoptosis on tumor cell lines. The most potent reversible acetylcholinesterase (AChE) inhibitors were Pt2, Pt4, and Pt5. Pt1 showed similar inhibitory potential toward AChE as cisplatin, but a different type of inhibition, which could contribute to lower neurotoxicity. Docking studies revealed that Pt2 and Pt4 were bound to the active gorge above the catalytic triad. In contrast, the other complexes were bound to the edge of the active gorge without impeding the approach to the catalytic triad. According to this, Pt1 represents a promising compound with potent anticancer properties, high selectivity, and low neurotoxicity.",
journal = "Chemico-Biological Interactions",
title = "Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action",
pages = "109708",
doi = "10.1016/j.cbi.2021.109708"
}
Bondžić, A. M., Žakula, J. J., Korićanac, L. B., Keta, O. D., Janjić, G. V., Đorđević, I. S.,& Rajković, S. U.. (2021). Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action. in Chemico-Biological Interactions, 109708.
https://doi.org/10.1016/j.cbi.2021.109708
Bondžić AM, Žakula JJ, Korićanac LB, Keta OD, Janjić GV, Đorđević IS, Rajković SU. Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action. in Chemico-Biological Interactions. 2021;:109708.
doi:10.1016/j.cbi.2021.109708 .
Bondžić, Aleksandra M., Žakula, Jelena J., Korićanac, Lela B., Keta, Otilija D., Janjić, Goran V., Đorđević, Ivana S., Rajković, Snežana U., "Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action" in Chemico-Biological Interactions (2021):109708,
https://doi.org/10.1016/j.cbi.2021.109708 . .

A Supramolecular Perspective of Coordination Effects on Fluorine Interactions

Petković Benazzouz, Marija M.; Rakić, Aleksandra A.; Trišović, Nemanja P.; Zarić, Božidarka; Janjić, Goran V.

(2021)

TY  - DATA
AU  - Petković Benazzouz, Marija M.
AU  - Rakić, Aleksandra A.
AU  - Trišović, Nemanja P.
AU  - Zarić, Božidarka
AU  - Janjić, Goran V.
PY  - 2021
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9996
AB  - Statistical analysis of the geometric parameters used for the description of noncovalent interactions involving the fluorine atom in crystal structures extracted from the CSD, the crystal packing, the model systems extracted from the crystal structure or obtained by reduction of the structures and interactions between different parts of the crystal structures (C−H/F, F/F, C−H/π, and F/π interactions), the total interaction energy, calculation of CCSD(T)/CBS interaction energies, Hartree−Fock energy and dispersion energy calculated at model system extracted from the crystal structure with refcode MINMAZ, and the analysis of the topological parame- ters by quantum theory of atoms in molecules (QTAIM).
T2  - Crystal Growth & Design
T1  - A Supramolecular Perspective of Coordination Effects on Fluorine Interactions
VL  - 21
IS  - 11
SP  - SI 001
DO  - 10.1021/acs.cgd.1c00584
ER  - 
@misc{
author = "Petković Benazzouz, Marija M. and Rakić, Aleksandra A. and Trišović, Nemanja P. and Zarić, Božidarka and Janjić, Goran V.",
year = "2021",
abstract = "Statistical analysis of the geometric parameters used for the description of noncovalent interactions involving the fluorine atom in crystal structures extracted from the CSD, the crystal packing, the model systems extracted from the crystal structure or obtained by reduction of the structures and interactions between different parts of the crystal structures (C−H/F, F/F, C−H/π, and F/π interactions), the total interaction energy, calculation of CCSD(T)/CBS interaction energies, Hartree−Fock energy and dispersion energy calculated at model system extracted from the crystal structure with refcode MINMAZ, and the analysis of the topological parame- ters by quantum theory of atoms in molecules (QTAIM).",
journal = "Crystal Growth & Design",
title = "A Supramolecular Perspective of Coordination Effects on Fluorine Interactions",
volume = "21",
number = "11",
pages = "SI 001",
doi = "10.1021/acs.cgd.1c00584"
}
Petković Benazzouz, M. M., Rakić, A. A., Trišović, N. P., Zarić, B.,& Janjić, G. V.. (2021). A Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth & Design, 21(11), SI 001.
https://doi.org/10.1021/acs.cgd.1c00584
Petković Benazzouz MM, Rakić AA, Trišović NP, Zarić B, Janjić GV. A Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth & Design. 2021;21(11):SI 001.
doi:10.1021/acs.cgd.1c00584 .
Petković Benazzouz, Marija M., Rakić, Aleksandra A., Trišović, Nemanja P., Zarić, Božidarka, Janjić, Goran V., "A Supramolecular Perspective of Coordination Effects on Fluorine Interactions" in Crystal Growth & Design, 21, no. 11 (2021):SI 001,
https://doi.org/10.1021/acs.cgd.1c00584 . .
1

Supramolecular Perspective of Coordination Effects on Fluorine Interactions

Petković Benazzouz, Marija M.; Rakić, Aleksandra A.; Trišović, Nemanja P.; Zarić, Božidarka; Janjić, Goran V.

(2021)

TY  - JOUR
AU  - Petković Benazzouz, Marija M.
AU  - Rakić, Aleksandra A.
AU  - Trišović, Nemanja P.
AU  - Zarić, Božidarka
AU  - Janjić, Goran V.
PY  - 2021
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9989
AB  - Coordination effects have been considered through the most common interactions in the crystal structures of fluoro compounds (C-H/F and F/F interactions). The supramolecular profile of these effects is based on quantum-chemical calculations for the assessment of the interaction strength and electrostatic potential maps, which provide a qualitative insight into the examined effect. Coordination of aliphatic fluorides leads to an increase of the negative potential of the F atoms, and, hence, an increase in the hydrogen-bonding acceptor ability (strengthening of C-H/F interactions) and a weakening of the F/F interactions, due to an increase in repulsive interactions between the F atoms. There is no significant change in the potential of the F atoms due to coordination of C6-aromatic fluorides, as in the case of aliphatic ones. This results in slight changes in the strengths of the C-H/F and F/F interactions (coupled with parallel interaction at large offsets, PILO), in a noticeable enhancement of stacking interactions, as well as in a significant enhancement of interactions involving the π-system (F/πand C-H/πinteractions). It has also been shown that a decrease in the charge of the metal ions leads to a decrease in the negative potential of the F atom and also that the nature of the metal ion has a significant influence on the value of the potential of the F atoms.
T2  - Crystal Growth & Design
T1  - Supramolecular Perspective of Coordination Effects on Fluorine Interactions
VL  - 21
IS  - 11
SP  - 6129
EP  - 6142
DO  - 10.1021/acs.cgd.1c00584
ER  - 
@article{
author = "Petković Benazzouz, Marija M. and Rakić, Aleksandra A. and Trišović, Nemanja P. and Zarić, Božidarka and Janjić, Goran V.",
year = "2021",
abstract = "Coordination effects have been considered through the most common interactions in the crystal structures of fluoro compounds (C-H/F and F/F interactions). The supramolecular profile of these effects is based on quantum-chemical calculations for the assessment of the interaction strength and electrostatic potential maps, which provide a qualitative insight into the examined effect. Coordination of aliphatic fluorides leads to an increase of the negative potential of the F atoms, and, hence, an increase in the hydrogen-bonding acceptor ability (strengthening of C-H/F interactions) and a weakening of the F/F interactions, due to an increase in repulsive interactions between the F atoms. There is no significant change in the potential of the F atoms due to coordination of C6-aromatic fluorides, as in the case of aliphatic ones. This results in slight changes in the strengths of the C-H/F and F/F interactions (coupled with parallel interaction at large offsets, PILO), in a noticeable enhancement of stacking interactions, as well as in a significant enhancement of interactions involving the π-system (F/πand C-H/πinteractions). It has also been shown that a decrease in the charge of the metal ions leads to a decrease in the negative potential of the F atom and also that the nature of the metal ion has a significant influence on the value of the potential of the F atoms.",
journal = "Crystal Growth & Design",
title = "Supramolecular Perspective of Coordination Effects on Fluorine Interactions",
volume = "21",
number = "11",
pages = "6129-6142",
doi = "10.1021/acs.cgd.1c00584"
}
Petković Benazzouz, M. M., Rakić, A. A., Trišović, N. P., Zarić, B.,& Janjić, G. V.. (2021). Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth & Design, 21(11), 6129-6142.
https://doi.org/10.1021/acs.cgd.1c00584
Petković Benazzouz MM, Rakić AA, Trišović NP, Zarić B, Janjić GV. Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth & Design. 2021;21(11):6129-6142.
doi:10.1021/acs.cgd.1c00584 .
Petković Benazzouz, Marija M., Rakić, Aleksandra A., Trišović, Nemanja P., Zarić, Božidarka, Janjić, Goran V., "Supramolecular Perspective of Coordination Effects on Fluorine Interactions" in Crystal Growth & Design, 21, no. 11 (2021):6129-6142,
https://doi.org/10.1021/acs.cgd.1c00584 . .
1

Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents

Milojkov, Dušan V.; Silvestre, Oscar F.; Stanić, Vojislav; Janjić, Goran V.; Mutavdžić, Dragosav R.; Milanović, Marija M.; Nieder, Jana B.

(2020)

TY  - JOUR
AU  - Milojkov, Dušan V.
AU  - Silvestre, Oscar F.
AU  - Stanić, Vojislav
AU  - Janjić, Goran V.
AU  - Mutavdžić, Dragosav R.
AU  - Milanović, Marija M.
AU  - Nieder, Jana B.
PY  - 2020
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8529
AB  - Fluorapatite doped with rare-earth elements has a wide-range of biomedical applications. Here, a new type of fluorapatite nanocrystals doped with praseodymium (FAP-Pr) with excitation-emission profiles in visible part of the spectrum is fabricated. Energy levels of Pr3+ activator ion contain metastable multiplet states that offer the possibility of efficient multicolor emission lines in FAP nanocrystals. Three types of FAP-Pr nanocrystals with 0.1%, 0.5% and 1% atomic percent of Pr3+ (along with the undoped FAP control sample) are studied. Their novel chemical production method is described, the FAP-Pr nanocrystals structure, biocompatibility and the suitability for cell imaging are analyzed. Physicochemical characterization confirms crystals down to nanometer size. In addition, quantum-chemical calculation predicts that Pr3+ ions are incorporated into the FAP crystal lattice at Ca2 (6 h) sites. In vitro viability results shows that FAP-Pr nanocrystals are nontoxic to live cells. Additionally, the cell uptake of the FAP-Pr nanocrystals is studied using fluorescence-based widefield and confocal microscopy. The nanocrystals show characteristic green emission at 545 nm (3P0→3H5 transition of Pr3+ ion) and orange emission at 600 nm (1D2→3H4), which we use to discriminate from cell autofluorescence background. Orthogonal projections across 3D confocal stacks show that the nanocrystals are able to enter the cells positioning themselves within the cytoplasm. Overall, the new FAP-Pr nanocrystals are biocompatible and of the tested types, the 0.5% Pr3+ doped nanocrystals show the highest promise as a tracking nanoparticle probe for bioimaging applications. © 2019
T2  - Journal of Luminescence
T1  - Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents
VL  - 217
SP  - 116757
DO  - 10.1016/j.jlumin.2019.116757
ER  - 
@article{
author = "Milojkov, Dušan V. and Silvestre, Oscar F. and Stanić, Vojislav and Janjić, Goran V. and Mutavdžić, Dragosav R. and Milanović, Marija M. and Nieder, Jana B.",
year = "2020",
abstract = "Fluorapatite doped with rare-earth elements has a wide-range of biomedical applications. Here, a new type of fluorapatite nanocrystals doped with praseodymium (FAP-Pr) with excitation-emission profiles in visible part of the spectrum is fabricated. Energy levels of Pr3+ activator ion contain metastable multiplet states that offer the possibility of efficient multicolor emission lines in FAP nanocrystals. Three types of FAP-Pr nanocrystals with 0.1%, 0.5% and 1% atomic percent of Pr3+ (along with the undoped FAP control sample) are studied. Their novel chemical production method is described, the FAP-Pr nanocrystals structure, biocompatibility and the suitability for cell imaging are analyzed. Physicochemical characterization confirms crystals down to nanometer size. In addition, quantum-chemical calculation predicts that Pr3+ ions are incorporated into the FAP crystal lattice at Ca2 (6 h) sites. In vitro viability results shows that FAP-Pr nanocrystals are nontoxic to live cells. Additionally, the cell uptake of the FAP-Pr nanocrystals is studied using fluorescence-based widefield and confocal microscopy. The nanocrystals show characteristic green emission at 545 nm (3P0→3H5 transition of Pr3+ ion) and orange emission at 600 nm (1D2→3H4), which we use to discriminate from cell autofluorescence background. Orthogonal projections across 3D confocal stacks show that the nanocrystals are able to enter the cells positioning themselves within the cytoplasm. Overall, the new FAP-Pr nanocrystals are biocompatible and of the tested types, the 0.5% Pr3+ doped nanocrystals show the highest promise as a tracking nanoparticle probe for bioimaging applications. © 2019",
journal = "Journal of Luminescence",
title = "Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents",
volume = "217",
pages = "116757",
doi = "10.1016/j.jlumin.2019.116757"
}
Milojkov, D. V., Silvestre, O. F., Stanić, V., Janjić, G. V., Mutavdžić, D. R., Milanović, M. M.,& Nieder, J. B.. (2020). Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents. in Journal of Luminescence, 217, 116757.
https://doi.org/10.1016/j.jlumin.2019.116757
Milojkov DV, Silvestre OF, Stanić V, Janjić GV, Mutavdžić DR, Milanović MM, Nieder JB. Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents. in Journal of Luminescence. 2020;217:116757.
doi:10.1016/j.jlumin.2019.116757 .
Milojkov, Dušan V., Silvestre, Oscar F., Stanić, Vojislav, Janjić, Goran V., Mutavdžić, Dragosav R., Milanović, Marija M., Nieder, Jana B., "Fabrication and characterization of luminescent Pr3+ doped fluorapatite nanocrystals as bioimaging contrast agents" in Journal of Luminescence, 217 (2020):116757,
https://doi.org/10.1016/j.jlumin.2019.116757 . .
9
6

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

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

(2020)

TY  - JOUR
AU  - Bondžić, Aleksandra
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 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., 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 A, 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, 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 . .
7

Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method

Milojkov, Dušan V.; Stanić, Vojislav; Dimović, Slavko; Mutavdžić, Dragosav R.; Živković-Radovanović, Vukosava; Janjić, Goran V.; Radotić, Ksenija

(2019)

TY  - JOUR
AU  - Milojkov, Dušan V.
AU  - Stanić, Vojislav
AU  - Dimović, Slavko
AU  - Mutavdžić, Dragosav R.
AU  - Živković-Radovanović, Vukosava
AU  - Janjić, Goran V.
AU  - Radotić, Ksenija
PY  - 2019
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8629
AB  - In the present study we have analyzed effects of Ag+ ions doping on energetic profiles of nanophosphors materials based on fluorapatite crystal system. The UV radiation absorption and luminescence properties of monophase fluorapatite (FAP) and Ag+ doped fluorapatite (AgFAP) nanomaterials obtained by neutralization method were investigated using the photoluminescence spectrophotometry. The excitation-emission profiles of nanomaterials were analyzed statistically by MCR-ALS method and number of fluorophores was extracted. FAP lattice absorbed light at 350 nm in the UVA part of spectrum, and with increasing concentration of Ag+ ions new absorption maximum appeared at 270 nm in the UVC part. Fluorescence of FAP nanoparticles was in violet region of visible part of the spectrum, with a red shift to the green region when Ag+ was doped in lattice. MCR-ALS analyses of fluorescence spectra confirm formation of two maxima, at 484 and 505 nm, as a consequence of Ag+ ions doping in FAP lattice at Ca1 (4f) sites. The results of quantum chemical calculations showed that an Ag+ ion is stronger bonded to the binding site 1 (-1352:6 kcal/mol) than to the binding site 2 (-1249:0 kcal/mol). Considering that AgFAP1 nanopowder absorbs photons over all part of UV radiation spectrum, this material might be used as potential radiation protective nanomaterial. © 2019 Polish Academy of Sciences. All rights reserved.
T2  - Acta Physica Polonica A
T1  - Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method
VL  - 136
IS  - 1
SP  - 86
EP  - 91
DO  - 10.12693/APhysPolA.136.86
ER  - 
@article{
author = "Milojkov, Dušan V. and Stanić, Vojislav and Dimović, Slavko and Mutavdžić, Dragosav R. and Živković-Radovanović, Vukosava and Janjić, Goran V. and Radotić, Ksenija",
year = "2019",
abstract = "In the present study we have analyzed effects of Ag+ ions doping on energetic profiles of nanophosphors materials based on fluorapatite crystal system. The UV radiation absorption and luminescence properties of monophase fluorapatite (FAP) and Ag+ doped fluorapatite (AgFAP) nanomaterials obtained by neutralization method were investigated using the photoluminescence spectrophotometry. The excitation-emission profiles of nanomaterials were analyzed statistically by MCR-ALS method and number of fluorophores was extracted. FAP lattice absorbed light at 350 nm in the UVA part of spectrum, and with increasing concentration of Ag+ ions new absorption maximum appeared at 270 nm in the UVC part. Fluorescence of FAP nanoparticles was in violet region of visible part of the spectrum, with a red shift to the green region when Ag+ was doped in lattice. MCR-ALS analyses of fluorescence spectra confirm formation of two maxima, at 484 and 505 nm, as a consequence of Ag+ ions doping in FAP lattice at Ca1 (4f) sites. The results of quantum chemical calculations showed that an Ag+ ion is stronger bonded to the binding site 1 (-1352:6 kcal/mol) than to the binding site 2 (-1249:0 kcal/mol). Considering that AgFAP1 nanopowder absorbs photons over all part of UV radiation spectrum, this material might be used as potential radiation protective nanomaterial. © 2019 Polish Academy of Sciences. All rights reserved.",
journal = "Acta Physica Polonica A",
title = "Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method",
volume = "136",
number = "1",
pages = "86-91",
doi = "10.12693/APhysPolA.136.86"
}
Milojkov, D. V., Stanić, V., Dimović, S., Mutavdžić, D. R., Živković-Radovanović, V., Janjić, G. V.,& Radotić, K.. (2019). Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method. in Acta Physica Polonica A, 136(1), 86-91.
https://doi.org/10.12693/APhysPolA.136.86
Milojkov DV, Stanić V, Dimović S, Mutavdžić DR, Živković-Radovanović V, Janjić GV, Radotić K. Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method. in Acta Physica Polonica A. 2019;136(1):86-91.
doi:10.12693/APhysPolA.136.86 .
Milojkov, Dušan V., Stanić, Vojislav, Dimović, Slavko, Mutavdžić, Dragosav R., Živković-Radovanović, Vukosava, Janjić, Goran V., Radotić, Ksenija, "Effects of Ag + Ion Doping on UV Radiation Absorption and Luminescence Profiles of Fluorapatite Nanomaterials Obtained by Neutralization Method" in Acta Physica Polonica A, 136, no. 1 (2019):86-91,
https://doi.org/10.12693/APhysPolA.136.86 . .
1
1
1

Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins

Nišavić, Marija; Janjić, Goran V.; Hozić, Amela; Petković, Marijana; Milčić, Miloš K.; Vujčić, Zoran; Cindrić, Mario

(2018)

TY  - JOUR
AU  - Nišavić, Marija
AU  - Janjić, Goran V.
AU  - Hozić, Amela
AU  - Petković, Marijana
AU  - Milčić, Miloš K.
AU  - Vujčić, Zoran
AU  - Cindrić, Mario
PY  - 2018
UR  - http://xlink.rsc.org/?DOI=C7MT00330G
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7615
AB  - Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.
T2  - Metallomics
T1  - Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins
VL  - 10
IS  - 4
SP  - 587
EP  - 594
DO  - 10.1039/C7MT00330G
ER  - 
@article{
author = "Nišavić, Marija and Janjić, Goran V. and Hozić, Amela and Petković, Marijana and Milčić, Miloš K. and Vujčić, Zoran and Cindrić, Mario",
year = "2018",
abstract = "Binding of three ruthenium(ii) compounds of general formula mer-[Ru(L3)(N-N)X][Y] (where L3 = 4-chloro-2,2:6,2-terpyridine (Cl-tpy); N-N = 1,2-diaminoethane (en), 1,2-diaminocyclohexane (dach) or 2,2-bipyridine (bipy); X = Cl; Y = Cl) to human serum albumin (HSA) has been investigated by nano-LC/nano-ESI MS and docking studies. A bottom-up proteomics approach has been applied for the structural characterization of metallated proteins and the data were analyzed in both the positive and negative ion mode. The negative ion mode was achieved after the post-column addition of an isopropanol solution of formaldehyde that enabled sample ionization at micro-flow rates. The negative ion mode MS has been proved to be beneficial for the analysis of binding sites on ruthenated protein in terms of ion charge reduction and consequent simplification of target sequence identification based on isotopic differences between ruthenated and non-ruthenated peptides. Moreover, the negative ion mode ESI MS shows the advantage of singly charged ion formation and, unlike MALDI MS, it does not cause complete ligand fragmentation, merging the benefits of each method into a single experiment. Six target sequences were identified for the binding of en and dach compounds, and four sequences for the binding of bipy. All compounds have been found to bind histidine and one aspartate residue. Docking studies showed that the identified sequences are the constituents of five distinct binding sites for en and dach, or two sites for the bipy complex. The selection of binding sites seems to be dependent on the chelate ligand and the form of the complex prior or after hydrolysis of the leaving chloride ligand.",
journal = "Metallomics",
title = "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins",
volume = "10",
number = "4",
pages = "587-594",
doi = "10.1039/C7MT00330G"
}
Nišavić, M., Janjić, G. V., Hozić, A., Petković, M., Milčić, M. K., Vujčić, Z.,& Cindrić, M.. (2018). Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics, 10(4), 587-594.
https://doi.org/10.1039/C7MT00330G
Nišavić M, Janjić GV, Hozić A, Petković M, Milčić MK, Vujčić Z, Cindrić M. Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins. in Metallomics. 2018;10(4):587-594.
doi:10.1039/C7MT00330G .
Nišavić, Marija, Janjić, Goran V., Hozić, Amela, Petković, Marijana, Milčić, Miloš K., Vujčić, Zoran, Cindrić, Mario, "Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins" in Metallomics, 10, no. 4 (2018):587-594,
https://doi.org/10.1039/C7MT00330G . .
1
8
6
7

Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites

Vujačić Nikezić, Ana V.; Janjić, Goran V.; Bondžić, Aleksandra; Zarić, Božidarka; Vasić Anićijević, Dragana D.; Momić, Tatjana; Vasić, Vesna M.

(2018)

TY  - JOUR
AU  - Vujačić Nikezić, Ana V.
AU  - Janjić, Goran V.
AU  - Bondžić, Aleksandra
AU  - Zarić, Božidarka
AU  - Vasić Anićijević, Dragana D.
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2018
UR  - http://xlink.rsc.org/?DOI=C8MT00111A
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7812
AB  - The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4]-, [AuCl2(dmso)2]+, [AuCl2(bipy)]+) and Pt(ii) ([PtCl2(dmso)2]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4]- and [PtCl2(dmso)2] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.
T2  - Metallomics
T1  - Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites
VL  - 10
IS  - 7
SP  - 1003
EP  - 1015
DO  - 10.1039/C8MT00111A
ER  - 
@article{
author = "Vujačić Nikezić, Ana V. and Janjić, Goran V. and Bondžić, Aleksandra and Zarić, Božidarka and Vasić Anićijević, Dragana D. and Momić, Tatjana and Vasić, Vesna M.",
year = "2018",
abstract = "The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4]-, [AuCl2(dmso)2]+, [AuCl2(bipy)]+) and Pt(ii) ([PtCl2(dmso)2]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4]- and [PtCl2(dmso)2] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.",
journal = "Metallomics",
title = "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites",
volume = "10",
number = "7",
pages = "1003-1015",
doi = "10.1039/C8MT00111A"
}
Vujačić Nikezić, A. V., Janjić, G. V., Bondžić, A., Zarić, B., Vasić Anićijević, D. D., Momić, T.,& Vasić, V. M.. (2018). Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics, 10(7), 1003-1015.
https://doi.org/10.1039/C8MT00111A
Vujačić Nikezić AV, Janjić GV, Bondžić A, Zarić B, Vasić Anićijević DD, Momić T, Vasić VM. Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics. 2018;10(7):1003-1015.
doi:10.1039/C8MT00111A .
Vujačić Nikezić, Ana V., Janjić, Goran V., Bondžić, Aleksandra, Zarić, Božidarka, Vasić Anićijević, Dragana D., Momić, Tatjana, Vasić, Vesna M., "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites" in Metallomics, 10, no. 7 (2018):1003-1015,
https://doi.org/10.1039/C8MT00111A . .
2
2
2

The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach

Bondžić, Aleksandra; Čolović, Mirjana B.; Janjić, Goran V.; Zarić, Božidarka; Petrović, Sandra; Krstić, Danijela Z.; Marzo, Tiziano; Messori, Luigi; Vasić, Vesna M.

(2017)

TY  - JOUR
AU  - Bondžić, Aleksandra
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 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., 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 A, 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, 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 . .
4
4

Na/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(III) complexes

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

(2017)

TY  - JOUR
AU  - Bondžić, Aleksandra
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 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., 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 A, 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, 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 . .
11
11

Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase

Nastasijević, Branislav J.; Milošević, Maja; Janjić, Goran V.; Stanić, Vojislav; Vasić, Vesna M.

(2016)

TY  - JOUR
AU  - Nastasijević, Branislav J.
AU  - Milošević, Maja
AU  - Janjić, Goran V.
AU  - Stanić, Vojislav
AU  - Vasić, Vesna M.
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1197
AB  - The extracellular nucleotides act as neurotransmitters and signaling molecules in CNS, binding to a P2X and P2Y receptors. Their concentration regulates a cascade of membrane ecto enzymes, including the ecto-nucleotide triphosphate diphosphohydrolases (E-NTPDases). In many neuropathological conditions, such as neuroinflammatory, epilepsy, depression and migraine, altering of E-NTPDase activity was observed. The objective of this study was to investigate whether Gentiana lutea (G. lutea) extracts affect E-NTPDase activity and which of their constituents (loganic acid, gentiopicroside, isovitexin, amarogentin and isogentisin) exert inhibitory activity. The constituents concentration in the extracts was determined by ultra performance liquid chromatography coupled with mass spectrometry (UPLC-MS). Extracts and constituents were tested with E-NTPDase displayed on the rat synaptosomal membrane as well as by molecular docking study. Ethanol water extract (50%, v/v) exerted significant level of inhibition (52%) at concentration of 200 mg mL(-1). By inhibition studies with single constituents about 30% inhibition was achieved in any case, thus the model of one substrate acting on two enzymes was used to determine IC50 values. Molecular docking study revealed amarogentin, isovitexin and isogentisin dimer as the potent E-NTPDase inhibitors with the binding energies ranging from -9.4 to -10 kcal mol(-1) versus -8.0 kcal mol(-1) for ATP. Presence of isogentisin only in ethanol water extracts may explain their better inhibitory acitivities. Findings of this study are useful from the perspective of safety of products based on G. lutea extracts, while investigated constituents belong to secoiridoids and xanthones class of compounds could be considered as a source of potential E-NTPDase inhibitors.
T2  - International Journal of Pharmacology
T1  - Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase
VL  - 12
IS  - 4
SP  - 272
EP  - 289
DO  - 10.3923/ijp.2016.272.289
ER  - 
@article{
author = "Nastasijević, Branislav J. and Milošević, Maja and Janjić, Goran V. and Stanić, Vojislav and Vasić, Vesna M.",
year = "2016",
abstract = "The extracellular nucleotides act as neurotransmitters and signaling molecules in CNS, binding to a P2X and P2Y receptors. Their concentration regulates a cascade of membrane ecto enzymes, including the ecto-nucleotide triphosphate diphosphohydrolases (E-NTPDases). In many neuropathological conditions, such as neuroinflammatory, epilepsy, depression and migraine, altering of E-NTPDase activity was observed. The objective of this study was to investigate whether Gentiana lutea (G. lutea) extracts affect E-NTPDase activity and which of their constituents (loganic acid, gentiopicroside, isovitexin, amarogentin and isogentisin) exert inhibitory activity. The constituents concentration in the extracts was determined by ultra performance liquid chromatography coupled with mass spectrometry (UPLC-MS). Extracts and constituents were tested with E-NTPDase displayed on the rat synaptosomal membrane as well as by molecular docking study. Ethanol water extract (50%, v/v) exerted significant level of inhibition (52%) at concentration of 200 mg mL(-1). By inhibition studies with single constituents about 30% inhibition was achieved in any case, thus the model of one substrate acting on two enzymes was used to determine IC50 values. Molecular docking study revealed amarogentin, isovitexin and isogentisin dimer as the potent E-NTPDase inhibitors with the binding energies ranging from -9.4 to -10 kcal mol(-1) versus -8.0 kcal mol(-1) for ATP. Presence of isogentisin only in ethanol water extracts may explain their better inhibitory acitivities. Findings of this study are useful from the perspective of safety of products based on G. lutea extracts, while investigated constituents belong to secoiridoids and xanthones class of compounds could be considered as a source of potential E-NTPDase inhibitors.",
journal = "International Journal of Pharmacology",
title = "Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase",
volume = "12",
number = "4",
pages = "272-289",
doi = "10.3923/ijp.2016.272.289"
}
Nastasijević, B. J., Milošević, M., Janjić, G. V., Stanić, V.,& Vasić, V. M.. (2016). Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase. in International Journal of Pharmacology, 12(4), 272-289.
https://doi.org/10.3923/ijp.2016.272.289
Nastasijević BJ, Milošević M, Janjić GV, Stanić V, Vasić VM. Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase. in International Journal of Pharmacology. 2016;12(4):272-289.
doi:10.3923/ijp.2016.272.289 .
Nastasijević, Branislav J., Milošević, Maja, Janjić, Goran V., Stanić, Vojislav, Vasić, Vesna M., "Gentiana lutea Extracts and their Constituents as Inhibitors of Synaptosomal Ecto-NTPDase" in International Journal of Pharmacology, 12, no. 4 (2016):272-289,
https://doi.org/10.3923/ijp.2016.272.289 . .
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5

CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors

Medaković, Vesna B.; Bogdanović, Goran A.; Milčić, Miloš K.; Janjić, Goran V.; Zarić, Snežana D.

(2012)

TY  - JOUR
AU  - Medaković, Vesna B.
AU  - Bogdanović, Goran A.
AU  - Milčić, Miloš K.
AU  - Janjić, Goran V.
AU  - Zarić, Snežana D.
PY  - 2012
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5184
AB  - CH/pi interactions in metal porphyrinato complexes were studied by analyzing data in crystal structures from the Cambridge Structural Database (CSD) and by quantum chemical calculations. The analysis of the data in the CSD shows that both five-membered pyrrole and six-membered chelate rings form CH/pi interactions. The interactions occur more frequently with five-membered rings. The analysis of distances in crystal structures and calculated energies show stronger interactions with six-membered chelate rings, indicating that a larger number of interactions with five-membered rings are not the consequence of stronger interactions, but better accessibility of five-membered pyrrole rings. The calculated energies of the interactions with positions in six-membered rings are -2.09 to -2.83 kcal/mol, while the energies with five-membered rings are -2.05 to -2.26 kcal/mol. The results reveal that stronger interactions of six-membered rings are the consequence of stronger electrostatic interactions. Substituents on the porphyrin ring significantly strengthen the interactions. Substituents on the six-membered ring strengthen the interaction energy by about 20%. The results show that CH/pi interactions play an important role in molecular recognition of metalloporphyrins. The significant influence of the substituents on interaction energies can be very important for the design of model systems in bioinorganic chemistry. (C) 2012 Elsevier Inc. All rights reserved.
T2  - Journal of Inorganic Biochemistry
T1  - CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors
VL  - 117
SP  - 157
EP  - 163
DO  - 10.1016/j.jinorgbio.2012.09.002
ER  - 
@article{
author = "Medaković, Vesna B. and Bogdanović, Goran A. and Milčić, Miloš K. and Janjić, Goran V. and Zarić, Snežana D.",
year = "2012",
abstract = "CH/pi interactions in metal porphyrinato complexes were studied by analyzing data in crystal structures from the Cambridge Structural Database (CSD) and by quantum chemical calculations. The analysis of the data in the CSD shows that both five-membered pyrrole and six-membered chelate rings form CH/pi interactions. The interactions occur more frequently with five-membered rings. The analysis of distances in crystal structures and calculated energies show stronger interactions with six-membered chelate rings, indicating that a larger number of interactions with five-membered rings are not the consequence of stronger interactions, but better accessibility of five-membered pyrrole rings. The calculated energies of the interactions with positions in six-membered rings are -2.09 to -2.83 kcal/mol, while the energies with five-membered rings are -2.05 to -2.26 kcal/mol. The results reveal that stronger interactions of six-membered rings are the consequence of stronger electrostatic interactions. Substituents on the porphyrin ring significantly strengthen the interactions. Substituents on the six-membered ring strengthen the interaction energy by about 20%. The results show that CH/pi interactions play an important role in molecular recognition of metalloporphyrins. The significant influence of the substituents on interaction energies can be very important for the design of model systems in bioinorganic chemistry. (C) 2012 Elsevier Inc. All rights reserved.",
journal = "Journal of Inorganic Biochemistry",
title = "CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors",
volume = "117",
pages = "157-163",
doi = "10.1016/j.jinorgbio.2012.09.002"
}
Medaković, V. B., Bogdanović, G. A., Milčić, M. K., Janjić, G. V.,& Zarić, S. D.. (2012). CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors. in Journal of Inorganic Biochemistry, 117, 157-163.
https://doi.org/10.1016/j.jinorgbio.2012.09.002
Medaković VB, Bogdanović GA, Milčić MK, Janjić GV, Zarić SD. CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors. in Journal of Inorganic Biochemistry. 2012;117:157-163.
doi:10.1016/j.jinorgbio.2012.09.002 .
Medaković, Vesna B., Bogdanović, Goran A., Milčić, Miloš K., Janjić, Goran V., Zarić, Snežana D., "CH/pi interactions in metal-porphyrin complexes with pyrrole and chelate rings as hydrogen acceptors" in Journal of Inorganic Biochemistry, 117 (2012):157-163,
https://doi.org/10.1016/j.jinorgbio.2012.09.002 . .
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