TY  - JOUR
AU  - Jovanović, Dunja
AU  - Filipović, Ana
AU  - Janjić, Goran
AU  - Lazarević-Pašti, Tamara
AU  - Džambaski, Zdravko
AU  - Bondžić, Bojan
AU  - Bondžić, Aleksandra
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7423
AB  - We have synthesized 22 C-1 functionalized-N-aryl-1,2,3,4-tetrahydroisoquinoline derivatives showing biological activities towards cholinergic enzymes. Synthesis was performed using visible-light-promoted photo-redox chemistry, starting from a common intermediate, and the application of this synthetic methodology drastically simplified synthetic routes and purification of desired compounds. All synthesized derivates were divided into four groups based on the substituents in the C-1 position, and their inhibition potencies towards two cholinergic enzymes, acetyl- and butyrylcholinesterase were evaluated. Most potent derivatives were selected, and kinetic analysis was further carried out to obtain insights into the mechanisms of inhibition of these two enzymes. Further validation of the mode of inhibition of cholinergic enzymes by the two most potent THIQ compounds, 3c and 3i, was performed using fluorescence-quenching titration studies. Molecular docking studies further confirmed the proposed mechanism of enzymes’ inhibition. In silico predictions of physicochemical properties, pharmacokinetics, drug-likeness, and medicinal chemistry friendliness of the selected most potent derivatives were performed using Swiss ADME tool. This was followed by UPLC-assisted log P determination and in vitro BBB permeability studies performed in order to assess the potential of the synthesized compounds to pass the BBB.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Targeting Alzheimer’s Disease: Evaluating the Efficacy of C-1 Functionalized N-Aryl-Tetrahydroisoquinolines as Cholinergic Enzyme Inhibitors and Promising Therapeutic Candidates
VL  - 25
IS  - 2
SP  - 1033
DO  - 10.3390/ijms25021033
ER  - 

@article{
author = "Jovanović, Dunja and Filipović, Ana and Janjić, Goran and Lazarević-Pašti, Tamara and Džambaski, Zdravko and Bondžić, Bojan and Bondžić, Aleksandra",
year = "2024",
abstract = "We have synthesized 22 C-1 functionalized-N-aryl-1,2,3,4-tetrahydroisoquinoline derivatives showing biological activities towards cholinergic enzymes. Synthesis was performed using visible-light-promoted photo-redox chemistry, starting from a common intermediate, and the application of this synthetic methodology drastically simplified synthetic routes and purification of desired compounds. All synthesized derivates were divided into four groups based on the substituents in the C-1 position, and their inhibition potencies towards two cholinergic enzymes, acetyl- and butyrylcholinesterase were evaluated. Most potent derivatives were selected, and kinetic analysis was further carried out to obtain insights into the mechanisms of inhibition of these two enzymes. Further validation of the mode of inhibition of cholinergic enzymes by the two most potent THIQ compounds, 3c and 3i, was performed using fluorescence-quenching titration studies. Molecular docking studies further confirmed the proposed mechanism of enzymes’ inhibition. In silico predictions of physicochemical properties, pharmacokinetics, drug-likeness, and medicinal chemistry friendliness of the selected most potent derivatives were performed using Swiss ADME tool. This was followed by UPLC-assisted log P determination and in vitro BBB permeability studies performed in order to assess the potential of the synthesized compounds to pass the BBB.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Targeting Alzheimer’s Disease: Evaluating the Efficacy of C-1 Functionalized N-Aryl-Tetrahydroisoquinolines as Cholinergic Enzyme Inhibitors and Promising Therapeutic Candidates",
volume = "25",
number = "2",
pages = "1033",
doi = "10.3390/ijms25021033"
}

Jovanović, D., Filipović, A., Janjić, G., Lazarević-Pašti, T., Džambaski, Z., Bondžić, B.,& Bondžić, A.. (2024). Targeting Alzheimer’s Disease: Evaluating the Efficacy of C-1 Functionalized N-Aryl-Tetrahydroisoquinolines as Cholinergic Enzyme Inhibitors and Promising Therapeutic Candidates. in International Journal of Molecular Sciences
MDPI., 25(2), 1033.
https://doi.org/10.3390/ijms25021033

Jovanović D, Filipović A, Janjić G, Lazarević-Pašti T, Džambaski Z, Bondžić B, Bondžić A. Targeting Alzheimer’s Disease: Evaluating the Efficacy of C-1 Functionalized N-Aryl-Tetrahydroisoquinolines as Cholinergic Enzyme Inhibitors and Promising Therapeutic Candidates. in International Journal of Molecular Sciences. 2024;25(2):1033.
doi:10.3390/ijms25021033 .

Jovanović, Dunja, Filipović, Ana, Janjić, Goran, Lazarević-Pašti, Tamara, Džambaski, Zdravko, Bondžić, Bojan, Bondžić, Aleksandra, "Targeting Alzheimer’s Disease: Evaluating the Efficacy of C-1 Functionalized N-Aryl-Tetrahydroisoquinolines as Cholinergic Enzyme Inhibitors and Promising Therapeutic Candidates" in International Journal of Molecular Sciences, 25, no. 2 (2024):1033,
https://doi.org/10.3390/ijms25021033 . .

TY  - CONF
AU  - Jovanović, Dunja
AU  - Filipović, Ana
AU  - Bondžić, Bojan
AU  - Bondžić, Aleksandra
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7087
AB  - Alzheimer's disease (AD), the most common form of dementia, is a progressive neurological disorder characterized by losing memory and other intellectual abilities that are serious enough to interfere with daily life. The disease is associated with loss of cholinergic neurons in the brain and the decreased level of ACh. In order to raise the ACh level in the brain the acetylcholinesterase (AChE) inhibitors have been applied as relevant drugs in the AD therapy. On the other hand, these inhibitors treat and improve only symptoms indicating necessity for new better therapies. One of them could be based on the inhibition of butyrylcholinesterase (BuChE) because of its increased activity during late stage of AD. Therefore, the BuChE inhibitors should be of great importance in therapy. 1,2,3,4-tetrahydroisoquinolines (THIQ) are a large group of natural and synthetic compounds which exert diverse biological activities against various infectious 
pathogens and neurodegenerative disorders. Due to these reasons, the THIQ have attracted a lot of attention in the scientific community which has resulted in the development of novel THIQ analogues with more potent biological activity. In this study the inhibitory potency of derivates of N-phenyl-1,2,3,4-
tetrahydroisoquinoline, 178, 196 and 202, were investigated toward two cholinergic enzymes, AChE and BuChE. The performed screening tests pointed out the different inhibition potency of the selected compounds toward both enzymes which was related with their structures. The most potent compound has been 178 with IC50 values 1.30 μM and 2.50 μM toward AChE and BuChE, respectively. However, no selectivity was observed. Introducing F-atom in the para position of N-phenyl group of the compound 178, the compound 202 was obtained. In this way, the selectivity was increased towards acetylcholinesterase without significant influence on the IC50 value. However, introducing a methoxy groups in the position C3 and C4 of the tetrahydroisoquinoline’s ring of 202, the compound 196 with decreased inhibitory activity was obtained. IC50 value of 196 was one order of magnitude higher compared with compound 202. Based on the obtained results it is possible to conclude that introducing F atom in the para position of the phenyl ring lead to increased selectivity of the investigated compounds while introducing methoxy group in the position of C3 and C4 of 
tetrahydroisoquinoline ring leads to decrease of their inhibitory potency.
PB  - Niš, Serbia : RAD Centre
C3  - Book of Abstracts - 11th International Conference on Radiation, Natural Science, Medicine, Engineering, Technology and Ecology, June 19-23, Herceg Novi, Montenegro
T1  - Influence of the structures of THIQ derivatives on their inhibitory properties toward acetyl - and butyrylcholinesterase
SP  - 134
EP  - 134
DO  - 10.21175/rad.abstr.book.2023.23.2
ER  - 

@conference{
author = "Jovanović, Dunja and Filipović, Ana and Bondžić, Bojan and Bondžić, Aleksandra",
year = "2023",
abstract = "Alzheimer's disease (AD), the most common form of dementia, is a progressive neurological disorder characterized by losing memory and other intellectual abilities that are serious enough to interfere with daily life. The disease is associated with loss of cholinergic neurons in the brain and the decreased level of ACh. In order to raise the ACh level in the brain the acetylcholinesterase (AChE) inhibitors have been applied as relevant drugs in the AD therapy. On the other hand, these inhibitors treat and improve only symptoms indicating necessity for new better therapies. One of them could be based on the inhibition of butyrylcholinesterase (BuChE) because of its increased activity during late stage of AD. Therefore, the BuChE inhibitors should be of great importance in therapy. 1,2,3,4-tetrahydroisoquinolines (THIQ) are a large group of natural and synthetic compounds which exert diverse biological activities against various infectious 
pathogens and neurodegenerative disorders. Due to these reasons, the THIQ have attracted a lot of attention in the scientific community which has resulted in the development of novel THIQ analogues with more potent biological activity. In this study the inhibitory potency of derivates of N-phenyl-1,2,3,4-
tetrahydroisoquinoline, 178, 196 and 202, were investigated toward two cholinergic enzymes, AChE and BuChE. The performed screening tests pointed out the different inhibition potency of the selected compounds toward both enzymes which was related with their structures. The most potent compound has been 178 with IC50 values 1.30 μM and 2.50 μM toward AChE and BuChE, respectively. However, no selectivity was observed. Introducing F-atom in the para position of N-phenyl group of the compound 178, the compound 202 was obtained. In this way, the selectivity was increased towards acetylcholinesterase without significant influence on the IC50 value. However, introducing a methoxy groups in the position C3 and C4 of the tetrahydroisoquinoline’s ring of 202, the compound 196 with decreased inhibitory activity was obtained. IC50 value of 196 was one order of magnitude higher compared with compound 202. Based on the obtained results it is possible to conclude that introducing F atom in the para position of the phenyl ring lead to increased selectivity of the investigated compounds while introducing methoxy group in the position of C3 and C4 of 
tetrahydroisoquinoline ring leads to decrease of their inhibitory potency.",
publisher = "Niš, Serbia : RAD Centre",
journal = "Book of Abstracts - 11th International Conference on Radiation, Natural Science, Medicine, Engineering, Technology and Ecology, June 19-23, Herceg Novi, Montenegro",
title = "Influence of the structures of THIQ derivatives on their inhibitory properties toward acetyl - and butyrylcholinesterase",
pages = "134-134",
doi = "10.21175/rad.abstr.book.2023.23.2"
}

Jovanović, D., Filipović, A., Bondžić, B.,& Bondžić, A.. (2023). Influence of the structures of THIQ derivatives on their inhibitory properties toward acetyl - and butyrylcholinesterase. in Book of Abstracts - 11th International Conference on Radiation, Natural Science, Medicine, Engineering, Technology and Ecology, June 19-23, Herceg Novi, Montenegro
Niš, Serbia : RAD Centre., 134-134.
https://doi.org/10.21175/rad.abstr.book.2023.23.2

Jovanović D, Filipović A, Bondžić B, Bondžić A. Influence of the structures of THIQ derivatives on their inhibitory properties toward acetyl - and butyrylcholinesterase. in Book of Abstracts - 11th International Conference on Radiation, Natural Science, Medicine, Engineering, Technology and Ecology, June 19-23, Herceg Novi, Montenegro. 2023;:134-134.
doi:10.21175/rad.abstr.book.2023.23.2 .

Jovanović, Dunja, Filipović, Ana, Bondžić, Bojan, Bondžić, Aleksandra, "Influence of the structures of THIQ derivatives on their inhibitory properties toward acetyl - and butyrylcholinesterase" in Book of Abstracts - 11th International Conference on Radiation, Natural Science, Medicine, Engineering, Technology and Ecology, June 19-23, Herceg Novi, Montenegro (2023):134-134,
https://doi.org/10.21175/rad.abstr.book.2023.23.2 . .

TY  - JOUR
AU  - Filipović, Ana
AU  - Džambaski, Zdravko
AU  - Bondžić, Aleksandra
AU  - Bondžić, Bojan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7078
AB  - Visible light promoted photoredox catalyzed formation of α-amino radicals from cyclic tertiary amine compounds and their subsequent addition to Michael acceptors performed in flow conditions allowed access to a wide range of functionalized N-aryl-substituted tetrahydroisoquinolines (THIQs) and N-aryl-substituted tetrahydro-β-carbolines (THBCs). Visible light in conjunction with Ru(bpy)3Cl2 photocatalyst allowed the formation and high reactivities of α-amino radicals in flow conditions at room temperature. These reactions gave valuable products with high efficiencies; some previously unavailable reaction 
pathways photo or thermal reaction conditions; i.e. direct synthesis of 1-substituted (THBCs) via α-amino radical path were successfully realized in flow. The use of custom-made FEP tube microreactor proved to be the key to succesfull α-amino-radical formation and overall reaction performance in flow. Three types of light transparent custom-made microfluidic devices were tested, among them glass/silicon and FEP type reactor showed very good results in the conversion of tested compounds. Plausible reaction mechanism is proposed in accordance with known principles of photo activation of tertiary amines.
PB  - Springer
T2  - Photochemical & Photobiological Sciences
T1  - Visible-light promoted photoredox catalysis in Flow: Addition of biologically important α‑Amino radicals to Michael Acceptors
VL  - 22
SP  - 2259
EP  - 2270
DO  - 10.1007/s43630-023-00448-8
ER  - 

@article{
author = "Filipović, Ana and Džambaski, Zdravko and Bondžić, Aleksandra and Bondžić, Bojan",
year = "2023",
abstract = "Visible light promoted photoredox catalyzed formation of α-amino radicals from cyclic tertiary amine compounds and their subsequent addition to Michael acceptors performed in flow conditions allowed access to a wide range of functionalized N-aryl-substituted tetrahydroisoquinolines (THIQs) and N-aryl-substituted tetrahydro-β-carbolines (THBCs). Visible light in conjunction with Ru(bpy)3Cl2 photocatalyst allowed the formation and high reactivities of α-amino radicals in flow conditions at room temperature. These reactions gave valuable products with high efficiencies; some previously unavailable reaction 
pathways photo or thermal reaction conditions; i.e. direct synthesis of 1-substituted (THBCs) via α-amino radical path were successfully realized in flow. The use of custom-made FEP tube microreactor proved to be the key to succesfull α-amino-radical formation and overall reaction performance in flow. Three types of light transparent custom-made microfluidic devices were tested, among them glass/silicon and FEP type reactor showed very good results in the conversion of tested compounds. Plausible reaction mechanism is proposed in accordance with known principles of photo activation of tertiary amines.",
publisher = "Springer",
journal = "Photochemical & Photobiological Sciences",
title = "Visible-light promoted photoredox catalysis in Flow: Addition of biologically important α‑Amino radicals to Michael Acceptors",
volume = "22",
pages = "2259-2270",
doi = "10.1007/s43630-023-00448-8"
}

Filipović, A., Džambaski, Z., Bondžić, A.,& Bondžić, B.. (2023). Visible-light promoted photoredox catalysis in Flow: Addition of biologically important α‑Amino radicals to Michael Acceptors. in Photochemical & Photobiological Sciences
Springer., 22, 2259-2270.
https://doi.org/10.1007/s43630-023-00448-8

Filipović A, Džambaski Z, Bondžić A, Bondžić B. Visible-light promoted photoredox catalysis in Flow: Addition of biologically important α‑Amino radicals to Michael Acceptors. in Photochemical & Photobiological Sciences. 2023;22:2259-2270.
doi:10.1007/s43630-023-00448-8 .

Filipović, Ana, Džambaski, Zdravko, Bondžić, Aleksandra, Bondžić, Bojan, "Visible-light promoted photoredox catalysis in Flow: Addition of biologically important α‑Amino radicals to Michael Acceptors" in Photochemical & Photobiological Sciences, 22 (2023):2259-2270,
https://doi.org/10.1007/s43630-023-00448-8 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Jovanović, Dunja
AU  - Arsenijević, Nevena
AU  - Laban, Bojana
AU  - Lazarević Pašti, Tamara
AU  - Klekotka, Urszula
AU  - Bondžić, Bojan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5374
AB  - The study of the interactions between nanoparticles (NPs) and proteins has had a pivotal role in facilitating the understanding of biological effects and safe application of NPs after exposure to the physiological environment. Herein, for the first time, the interaction between L-methionine capped silver nanoparticles (AgMet), and bovine serum albumin (BSA) is investigated in order to predict the fate of AgMet after its contact with the most abundant blood transport protein. The detailed insights into the mechanism of interaction were achieved using different physicochemical techniques. The UV/Vis, TEM, and DLS were used for the characterization of the newly formed “entity”, while the kinetic and thermodynamic parameters were utilized to describe the adsorption process. Additionally, the fluorescence quenching and synchronous fluorescence studies enabled the prediction of the binding affinity and gave us insight into the influence of the adsorption on the conformation state of the BSA. According to the best of our knowledge, for the first time, we show that BSA can be used as an external stabilizer agent which is able to induce the peptization of previously agglomerated AgMet. We believe that the obtained results could contribute to further improvement of AgNPs’ performances as well as to the understanding of their in vivo behavior, which could contribute to their potential use in preclinical research studies.
PB  - Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - "Soft Protein Corona” as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction
VL  - 23
IS  - 16
SP  - 8985
DO  - 10.3390/ijms23168985
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Jovanović, Dunja and Arsenijević, Nevena and Laban, Bojana and Lazarević Pašti, Tamara and Klekotka, Urszula and Bondžić, Bojan",
year = "2022",
abstract = "The study of the interactions between nanoparticles (NPs) and proteins has had a pivotal role in facilitating the understanding of biological effects and safe application of NPs after exposure to the physiological environment. Herein, for the first time, the interaction between L-methionine capped silver nanoparticles (AgMet), and bovine serum albumin (BSA) is investigated in order to predict the fate of AgMet after its contact with the most abundant blood transport protein. The detailed insights into the mechanism of interaction were achieved using different physicochemical techniques. The UV/Vis, TEM, and DLS were used for the characterization of the newly formed “entity”, while the kinetic and thermodynamic parameters were utilized to describe the adsorption process. Additionally, the fluorescence quenching and synchronous fluorescence studies enabled the prediction of the binding affinity and gave us insight into the influence of the adsorption on the conformation state of the BSA. According to the best of our knowledge, for the first time, we show that BSA can be used as an external stabilizer agent which is able to induce the peptization of previously agglomerated AgMet. We believe that the obtained results could contribute to further improvement of AgNPs’ performances as well as to the understanding of their in vivo behavior, which could contribute to their potential use in preclinical research studies.",
publisher = "Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = ""Soft Protein Corona” as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction",
volume = "23",
number = "16",
pages = "8985",
doi = "10.3390/ijms23168985"
}

Bondžić, A. M., Jovanović, D., Arsenijević, N., Laban, B., Lazarević Pašti, T., Klekotka, U.,& Bondžić, B.. (2022). "Soft Protein Corona” as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction. in International Journal of Molecular Sciences
Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)., 23(16), 8985.
https://doi.org/10.3390/ijms23168985

Bondžić AM, Jovanović D, Arsenijević N, Laban B, Lazarević Pašti T, Klekotka U, Bondžić B. "Soft Protein Corona” as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction. in International Journal of Molecular Sciences. 2022;23(16):8985.
doi:10.3390/ijms23168985 .

Bondžić, Aleksandra M., Jovanović, Dunja, Arsenijević, Nevena, Laban, Bojana, Lazarević Pašti, Tamara, Klekotka, Urszula, Bondžić, Bojan, ""Soft Protein Corona” as the Stabilizer of the Methionine-Coated Silver Nanoparticles in the Physiological Environment: Insights into the Mechanism of the Interaction" in International Journal of Molecular Sciences, 23, no. 16 (2022):8985,
https://doi.org/10.3390/ijms23168985 . .

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  - Žakula, Jelena J.
AU  - Korićanac, Lela
AU  - Keta, Otilija D.
AU  - Janjić, Goran
AU  - Đorđević, Ivana S.
AU  - Rajković, Snežana
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5412
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.
PB  - Elsevier
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
VL  - 351
SP  - 109708
DO  - 10.1016/j.cbi.2021.109708
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Žakula, Jelena J. and Korićanac, Lela and Keta, Otilija D. and Janjić, Goran and Đorđević, Ivana S. and Rajković, Snežana",
year = "2022",
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.",
publisher = "Elsevier",
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",
volume = "351",
pages = "109708",
doi = "10.1016/j.cbi.2021.109708"
}

Bondžić, A. M., Žakula, J. J., Korićanac, L., Keta, O. D., Janjić, G., Đorđević, I. S.,& Rajković, S.. (2022). 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
Elsevier., 351, 109708.
https://doi.org/10.1016/j.cbi.2021.109708

Bondžić AM, Žakula JJ, Korićanac L, Keta OD, Janjić G, Đorđević IS, Rajković S. 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. 2022;351:109708.
doi:10.1016/j.cbi.2021.109708 .

Bondžić, Aleksandra M., Žakula, Jelena J., Korićanac, Lela, Keta, Otilija D., Janjić, Goran, Đorđević, Ivana S., Rajković, Snežana, "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, 351 (2022):109708,
https://doi.org/10.1016/j.cbi.2021.109708 . .

TY  - JOUR
AU  - Džambaski, Zdravko
AU  - Bondžić, Aleksandra M.
AU  - Triandafillidi, Ierasia
AU  - Kokotos, Christoforos G.
AU  - Bondžić, Bojan
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4823
AB  - Herein, we demonstrate that organic, single-electron oxidant in the presence of diarylprolinol silylether type catalyst serves as a tool for the transformation of electron-rich enamines to iminium ions. These iminium ions take part in a subsequent Michael-initiated ring-closure (MIRC) reaction with in situ present nucleophile giving rise to overall cyclopropanation reaction of saturated aldehydes. Stereodefined cyclopropanes are obtained in high yields and selectivities. This one-pot transformation represents the additional example of saturated aldehydes being used in the coupled one-pot processes. (Figure presented.).
PB  - Wiley
T2  - Advanced Synthesis and Catalysis
T1  - Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction
VL  - 363
IS  - 16
SP  - 4002
EP  - 4008
DO  - 10.1002/adsc.202100630
ER  - 

@article{
author = "Džambaski, Zdravko and Bondžić, Aleksandra M. and Triandafillidi, Ierasia and Kokotos, Christoforos G. and Bondžić, Bojan",
year = "2021",
abstract = "Herein, we demonstrate that organic, single-electron oxidant in the presence of diarylprolinol silylether type catalyst serves as a tool for the transformation of electron-rich enamines to iminium ions. These iminium ions take part in a subsequent Michael-initiated ring-closure (MIRC) reaction with in situ present nucleophile giving rise to overall cyclopropanation reaction of saturated aldehydes. Stereodefined cyclopropanes are obtained in high yields and selectivities. This one-pot transformation represents the additional example of saturated aldehydes being used in the coupled one-pot processes. (Figure presented.).",
publisher = "Wiley",
journal = "Advanced Synthesis and Catalysis",
title = "Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction",
volume = "363",
number = "16",
pages = "4002-4008",
doi = "10.1002/adsc.202100630"
}

Džambaski, Z., Bondžić, A. M., Triandafillidi, I., Kokotos, C. G.,& Bondžić, B.. (2021). Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction. in Advanced Synthesis and Catalysis
Wiley., 363(16), 4002-4008.
https://doi.org/10.1002/adsc.202100630

Džambaski Z, Bondžić AM, Triandafillidi I, Kokotos CG, Bondžić B. Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction. in Advanced Synthesis and Catalysis. 2021;363(16):4002-4008.
doi:10.1002/adsc.202100630 .

Džambaski, Zdravko, Bondžić, Aleksandra M., Triandafillidi, Ierasia, Kokotos, Christoforos G., Bondžić, Bojan, "Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction" in Advanced Synthesis and Catalysis, 363, no. 16 (2021):4002-4008,
https://doi.org/10.1002/adsc.202100630 . .

TY  - JOUR
AU  - Bondžić, Aleksandra
AU  - Senćanski, Milan
AU  - Vujačić Nikezić, Ana V.
AU  - Kirillova, Marina V.
AU  - André, Vânia
AU  - Kirillov, Alexander M.
AU  - Bondžić, Bojan
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3958
AB  - Three coordination compounds featuring different types of tetracopper(II) cores, namely
[O⊂Cu4{N(CH2CH2O)3}4(BOH)4][BF4]2 (1), [Cu4(μ4-H2edte)(μ5-H2edte)(sal)2]n·7nH2O, (H4edte=N,N,N′,
N′-tetrakis(2-hydroxyethyl)ethylenediamine, H2sal=salicylic acid) (2), and [{Cu4(μ3-Hbes)4(μ-hba)}K
(H2O)3]n, H3bes=N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (3), were assayed for their potency to
inhibit the acetyl (AChE) and butyrylcholinesterase (BuChE) enzymes aiming to test these compounds as potential
dual inhibitors in the treatment of Alzheimer's disease. All the investigated compounds showed a strong
inhibitory potency toward both enzymes with IC50 values in micromolar range of concentration; compound 1
displayed the most potent inhibitory behaviour toward both enzymes. The mechanism of the AChE and BuChE
inhibition was examined by enzyme kinetic measurements. The obtained kinetic parameters, Vmax and Km indicated
an uncompetitive type of inhibition of both enzymes by compound 1. For the other two compounds a
non-competitive inhibition mode was observed. To get further insight into the mechanism of action and to
elucidate binding modes in details we examined the interactions of 1–3 with acetylcholinesterase, using molecular
docking approach. Grid based docking studies indicated that these compounds can bind to peripheral
anionic site (PAS) of the AChE with Ki values in micromolar range. Moreover, blind docking revealed the
capability of investigated compounds to bind to new allosteric site (i.e. binding site II) distinct from PAS.
Showing that these Cu-based compounds can act as new allosteric inhibitors of AChE and identifying novel
allosteric binding site on AChE represents a significant contribution toward the design of novel and more
effective inhibitors of AChE.
PB  - Elsevier
T2  - Journal of Inorganic Biochemistry
T1  - Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action
VL  - 205
SP  - 110990
DO  - 10.1016/j.jinorgbio.2019.110990
ER  - 

@article{
author = "Bondžić, Aleksandra and Senćanski, Milan and Vujačić Nikezić, Ana V. and Kirillova, Marina V. and André, Vânia and Kirillov, Alexander M. and Bondžić, Bojan",
year = "2020",
abstract = "Three coordination compounds featuring different types of tetracopper(II) cores, namely
[O⊂Cu4{N(CH2CH2O)3}4(BOH)4][BF4]2 (1), [Cu4(μ4-H2edte)(μ5-H2edte)(sal)2]n·7nH2O, (H4edte=N,N,N′,
N′-tetrakis(2-hydroxyethyl)ethylenediamine, H2sal=salicylic acid) (2), and [{Cu4(μ3-Hbes)4(μ-hba)}K
(H2O)3]n, H3bes=N,N-bis(2-hydroxyethyl)-2-aminoethanesulfonic acid (3), were assayed for their potency to
inhibit the acetyl (AChE) and butyrylcholinesterase (BuChE) enzymes aiming to test these compounds as potential
dual inhibitors in the treatment of Alzheimer's disease. All the investigated compounds showed a strong
inhibitory potency toward both enzymes with IC50 values in micromolar range of concentration; compound 1
displayed the most potent inhibitory behaviour toward both enzymes. The mechanism of the AChE and BuChE
inhibition was examined by enzyme kinetic measurements. The obtained kinetic parameters, Vmax and Km indicated
an uncompetitive type of inhibition of both enzymes by compound 1. For the other two compounds a
non-competitive inhibition mode was observed. To get further insight into the mechanism of action and to
elucidate binding modes in details we examined the interactions of 1–3 with acetylcholinesterase, using molecular
docking approach. Grid based docking studies indicated that these compounds can bind to peripheral
anionic site (PAS) of the AChE with Ki values in micromolar range. Moreover, blind docking revealed the
capability of investigated compounds to bind to new allosteric site (i.e. binding site II) distinct from PAS.
Showing that these Cu-based compounds can act as new allosteric inhibitors of AChE and identifying novel
allosteric binding site on AChE represents a significant contribution toward the design of novel and more
effective inhibitors of AChE.",
publisher = "Elsevier",
journal = "Journal of Inorganic Biochemistry",
title = "Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action",
volume = "205",
pages = "110990",
doi = "10.1016/j.jinorgbio.2019.110990"
}

Bondžić, A., Senćanski, M., Vujačić Nikezić, A. V., Kirillova, M. V., André, V., Kirillov, A. M.,& Bondžić, B.. (2020). Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action. in Journal of Inorganic Biochemistry
Elsevier., 205, 110990.
https://doi.org/10.1016/j.jinorgbio.2019.110990

Bondžić A, Senćanski M, Vujačić Nikezić AV, Kirillova MV, André V, Kirillov AM, Bondžić B. Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action. in Journal of Inorganic Biochemistry. 2020;205:110990.
doi:10.1016/j.jinorgbio.2019.110990 .

Bondžić, Aleksandra, Senćanski, Milan, Vujačić Nikezić, Ana V., Kirillova, Marina V., André, Vânia, Kirillov, Alexander M., Bondžić, Bojan, "Aminoalcoholate-driven tetracopper(II) cores as dual acetyl and butyrylcholinesterase inhibitors: Experimental and theoretical elucidation of mechanism of action" in Journal of Inorganic Biochemistry, 205 (2020):110990,
https://doi.org/10.1016/j.jinorgbio.2019.110990 . .

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  - Vujačić Nikezić, Ana V.
AU  - Janjić, Goran
AU  - Bondžić, Aleksandra M.
AU  - Zarić, Božidarka
AU  - Vasic-Anicijevic, Dragana D.
AU  - Momic, Tatjana G.
AU  - Vasić, Vesna M.
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2452
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.
PB  - Royal Soc Chemistry, Cambridge
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 and Bondžić, Aleksandra M. and Zarić, Božidarka and Vasic-Anicijevic, Dragana D. and Momic, Tatjana G. 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.",
publisher = "Royal Soc Chemistry, Cambridge",
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., Bondžić, A. M., Zarić, B., Vasic-Anicijevic, D. D., Momic, T. G.,& 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
Royal Soc Chemistry, Cambridge., 10(7), 1003-1015.
https://doi.org/10.1039/c8mt00111a

Vujačić Nikezić AV, Janjić G, Bondžić AM, Zarić B, Vasic-Anicijevic DD, Momic TG, 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, Bondžić, Aleksandra M., Zarić, Božidarka, Vasic-Anicijevic, Dragana D., Momic, Tatjana G., 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 . .

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 . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Čolović, Mirjana B.
AU  - Janjić, Goran
AU  - Zarić, Božidarka
AU  - Petrović, Sandra
AU  - Krstic, Danijela Z.
AU  - Marzo, Tiziano
AU  - Messori, Luigi
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2143
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.
PB  - Springer, New York
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 and Zarić, Božidarka and Petrović, Sandra and Krstic, 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.",
publisher = "Springer, New York",
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., Zarić, B., Petrović, S., Krstic, 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
Springer, New York., 22(6), 819-832.
https://doi.org/10.1007/s00775-017-1460-5

Bondžić AM, Čolović MB, Janjić G, Zarić B, Petrović S, Krstic 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, Zarić, Božidarka, Petrović, Sandra, Krstic, 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  - Lazarević-Pašti, Tamara D.
AU  - Bondžić, Bojan
AU  - Čolović, Mirjana B.
AU  - Jadranin, Milka
AU  - Vasić, Vesna M.
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1293
AB  - The aim of the present paper was to investigate the reaction of quercetin, the flavonol very often used as a dietary supplement, with [AuCl4](-) ions. The reaction was studied spectrophotometrically using the equimolar solutions in 1 : 1 water-methanol at pH similar to 2. The spectrophotometric data indicated the formation of the products with an absorption maximum at 295 nm in all cases, characteristic of the oxidized forms of quercetin. HPLC coupled with DAD and LC-MS analysis of the reaction products suggested that the oxidation of quercetin resulted in the generation of similar metabolites including quinone and various oxidized quercetin-solvent adducts. In addition, cyclic voltammetric measurements confirmed that under applied experimental conditions, the reduction of Au(III) to Au(0) took place. The reduction species in the reaction mixture were Au(III) ions, while Au(I) disproportionates back to Au(III) and Au(0). The newly generated Au(III) ions further oxidized 3'-4'-dihydroxy groups of quercetin adducts obtained after first 2e(-) oxidation, giving the final reaction products. Based on the identification of reaction products, the reaction mechanism for the oxidation of quercetin in the presence of Au(III) which involves two 2e(-) transfer processes was proposed.
PB  - Royal Soc Chemistry, Cambridge
T2  - New Journal of Chemistry
T1  - Investigation of reaction between quercetin and Au(III) in acidic media: mechanism and identification of reaction products
VL  - 37
IS  - 4
SP  - 901
EP  - 908
DO  - 10.1039/c2nj40742f
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Lazarević-Pašti, Tamara D. and Bondžić, Bojan and Čolović, Mirjana B. and Jadranin, Milka and Vasić, Vesna M.",
year = "2013",
abstract = "The aim of the present paper was to investigate the reaction of quercetin, the flavonol very often used as a dietary supplement, with [AuCl4](-) ions. The reaction was studied spectrophotometrically using the equimolar solutions in 1 : 1 water-methanol at pH similar to 2. The spectrophotometric data indicated the formation of the products with an absorption maximum at 295 nm in all cases, characteristic of the oxidized forms of quercetin. HPLC coupled with DAD and LC-MS analysis of the reaction products suggested that the oxidation of quercetin resulted in the generation of similar metabolites including quinone and various oxidized quercetin-solvent adducts. In addition, cyclic voltammetric measurements confirmed that under applied experimental conditions, the reduction of Au(III) to Au(0) took place. The reduction species in the reaction mixture were Au(III) ions, while Au(I) disproportionates back to Au(III) and Au(0). The newly generated Au(III) ions further oxidized 3'-4'-dihydroxy groups of quercetin adducts obtained after first 2e(-) oxidation, giving the final reaction products. Based on the identification of reaction products, the reaction mechanism for the oxidation of quercetin in the presence of Au(III) which involves two 2e(-) transfer processes was proposed.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "New Journal of Chemistry",
title = "Investigation of reaction between quercetin and Au(III) in acidic media: mechanism and identification of reaction products",
volume = "37",
number = "4",
pages = "901-908",
doi = "10.1039/c2nj40742f"
}

Bondžić, A. M., Lazarević-Pašti, T. D., Bondžić, B., Čolović, M. B., Jadranin, M.,& Vasić, V. M.. (2013). Investigation of reaction between quercetin and Au(III) in acidic media: mechanism and identification of reaction products. in New Journal of Chemistry
Royal Soc Chemistry, Cambridge., 37(4), 901-908.
https://doi.org/10.1039/c2nj40742f

Bondžić AM, Lazarević-Pašti TD, Bondžić B, Čolović MB, Jadranin M, Vasić VM. Investigation of reaction between quercetin and Au(III) in acidic media: mechanism and identification of reaction products. in New Journal of Chemistry. 2013;37(4):901-908.
doi:10.1039/c2nj40742f .

Bondžić, Aleksandra M., Lazarević-Pašti, Tamara D., Bondžić, Bojan, Čolović, Mirjana B., Jadranin, Milka, Vasić, Vesna M., "Investigation of reaction between quercetin and Au(III) in acidic media: mechanism and identification of reaction products" in New Journal of Chemistry, 37, no. 4 (2013):901-908,
https://doi.org/10.1039/c2nj40742f . .

TY  - JOUR
AU  - Bondžić, Bojan
AU  - Džambaski, Zdravko
AU  - Bondžić, Aleksandra M.
AU  - Marković, Rade
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1126
AB  - The a-C position in 4-oxo thiazolidinones functions as one of the three possible nucleophilic sites in these molecules. We used the inherent reactivity of alpha-C of the exocyclic double bond (a so called push pull system) to obtain bicyclic fused thiazolidinones via pi-annulation cyclization. Appropriate reaction conditions to selectively activate this position and secondary nitrogen towards N, pi-annulation were found. Furthermore, the intramolecular vinylogous iminium ion 6-exo-trig cyclization was used to access fused bicyclic precursors for the pi-annulation in order to obtain the novel tricyclic structures stereoselectively.
PB  - Oxford : Pergamon-Elsevier Science Ltd
T2  - Tetrahedron
T1  - pi-Annulation reactions of 4-thiazolidinone enaminones in the synthesis of fused bi- and tri-cyclic compounds
VL  - 68
IS  - 47
SP  - 9556
EP  - 9565
DO  - 10.1016/j.tet.2012.09.080
ER  - 

@article{
author = "Bondžić, Bojan and Džambaski, Zdravko and Bondžić, Aleksandra M. and Marković, Rade",
year = "2012",
abstract = "The a-C position in 4-oxo thiazolidinones functions as one of the three possible nucleophilic sites in these molecules. We used the inherent reactivity of alpha-C of the exocyclic double bond (a so called push pull system) to obtain bicyclic fused thiazolidinones via pi-annulation cyclization. Appropriate reaction conditions to selectively activate this position and secondary nitrogen towards N, pi-annulation were found. Furthermore, the intramolecular vinylogous iminium ion 6-exo-trig cyclization was used to access fused bicyclic precursors for the pi-annulation in order to obtain the novel tricyclic structures stereoselectively.",
publisher = "Oxford : Pergamon-Elsevier Science Ltd",
journal = "Tetrahedron",
title = "pi-Annulation reactions of 4-thiazolidinone enaminones in the synthesis of fused bi- and tri-cyclic compounds",
volume = "68",
number = "47",
pages = "9556-9565",
doi = "10.1016/j.tet.2012.09.080"
}

Bondžić, B., Džambaski, Z., Bondžić, A. M.,& Marković, R.. (2012). pi-Annulation reactions of 4-thiazolidinone enaminones in the synthesis of fused bi- and tri-cyclic compounds. in Tetrahedron
Oxford : Pergamon-Elsevier Science Ltd., 68(47), 9556-9565.
https://doi.org/10.1016/j.tet.2012.09.080

Bondžić B, Džambaski Z, Bondžić AM, Marković R. pi-Annulation reactions of 4-thiazolidinone enaminones in the synthesis of fused bi- and tri-cyclic compounds. in Tetrahedron. 2012;68(47):9556-9565.
doi:10.1016/j.tet.2012.09.080 .

Bondžić, Bojan, Džambaski, Zdravko, Bondžić, Aleksandra M., Marković, Rade, "pi-Annulation reactions of 4-thiazolidinone enaminones in the synthesis of fused bi- and tri-cyclic compounds" in Tetrahedron, 68, no. 47 (2012):9556-9565,
https://doi.org/10.1016/j.tet.2012.09.080 . .