TY  - CONF
AU  - Jovanović, Dunja
AU  - Filipović, Ana
AU  - Bondžić, Bojan
AU  - Bondžić, Aleksandra
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12228
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 : RAD Centre
C3  - RAD 2023 : 11th International Conference on Radiation Natural Sciences, Medicine, Engineering, Technology and Ecology : Book of Abstracts
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 : RAD Centre",
journal = "RAD 2023 : 11th International Conference on Radiation Natural Sciences, Medicine, Engineering, Technology and Ecology : Book of Abstracts",
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 RAD 2023 : 11th International Conference on Radiation Natural Sciences, Medicine, Engineering, Technology and Ecology : Book of Abstracts
Niš : 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 RAD 2023 : 11th International Conference on Radiation Natural Sciences, Medicine, Engineering, Technology and Ecology : Book of Abstracts. 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 RAD 2023 : 11th International Conference on Radiation Natural Sciences, Medicine, Engineering, Technology and Ecology : Book of Abstracts (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 M.
AU  - Bondžić, Bojan P.
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11171
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.
T2  - Photochemical & Photobiological Sciences
T1  - Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors
DO  - 10.1007/s43630-023-00448-8
ER  - 

@article{
author = "Filipović, Ana and Džambaski, Zdravko and Bondžić, Aleksandra M. and Bondžić, Bojan P.",
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.",
journal = "Photochemical & Photobiological Sciences",
title = "Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors",
doi = "10.1007/s43630-023-00448-8"
}

Filipović, A., Džambaski, Z., Bondžić, A. M.,& Bondžić, B. P.. (2023). Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors. in Photochemical & Photobiological Sciences.
https://doi.org/10.1007/s43630-023-00448-8

Filipović A, Džambaski Z, Bondžić AM, Bondžić BP. Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors. in Photochemical & Photobiological Sciences. 2023;.
doi:10.1007/s43630-023-00448-8 .

Filipović, Ana, Džambaski, Zdravko, Bondžić, Aleksandra M., Bondžić, Bojan P., "Visible-light promoted photoredox catalysis in flow: addition of biologically important α‑amino radicals to michael acceptors" in Photochemical & Photobiological Sciences (2023),
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 P.
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10404
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.
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 P.",
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.",
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. P.. (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, 23(16), 8985.
https://doi.org/10.3390/ijms23168985

Bondžić AM, Jovanović D, Arsenijević N, Laban B, Lazarević-Pašti T, Klekotka U, Bondžić BP. “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 P., "“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 M.
AU  - Lazarević-Pašti, Tamara
AU  - Pašti, Igor A.
AU  - Bondžić, Bojan P.
AU  - Momčilović, Miloš
AU  - Loosen, Alexandra
AU  - Parac-Vogt, Tatjana N.
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10210
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.
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 M. and Lazarević-Pašti, Tamara and Pašti, Igor A. and Bondžić, Bojan P. and Momčilović, Miloš and Loosen, Alexandra and Parac-Vogt, Tatjana N.",
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.",
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. M., Lazarević-Pašti, T., Pašti, I. A., Bondžić, B. P., Momčilović, M., Loosen, A.,& Parac-Vogt, T. N.. (2022). Synergistic Effect of Sorption and Hydrolysis by NU-1000 Nanostructures for Removal and Detoxification of Chlorpyrifos. in ACS Applied Nano Materials, 5(3), 3312-3324.
https://doi.org/10.1021/acsanm.1c03863

Bondžić AM, Lazarević-Pašti T, Pašti IA, Bondžić BP, Momčilović M, Loosen A, Parac-Vogt TN. 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 M., Lazarević-Pašti, Tamara, Pašti, Igor A., Bondžić, Bojan P., Momčilović, Miloš, Loosen, Alexandra, Parac-Vogt, Tatjana N., "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  - Džambaski, Zdravko
AU  - Bondžić, Aleksandra M.
AU  - Triandafillidi, Ierasia
AU  - Kokotos, Christoforos G.
AU  - Bondžić, Bojan P.
PY  - 2021
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9871
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.).
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 P.",
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.).",
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. P.. (2021). Organocatalytic, Organic Oxidant Promoted, Enamine C−H Oxidation/Cyclopropanation Reaction. in Advanced Synthesis and Catalysis, 363(16), 4002-4008.
https://doi.org/10.1002/adsc.202100630

Džambaski Z, Bondžić AM, Triandafillidi I, Kokotos CG, Bondžić BP. 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 P., "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 M.
AU  - Senćanski, Milan V.
AU  - Vujačić Nikezić, Ana V.
AU  - Kirillova, Marina V.
AU  - André, Vania
AU  - Kirillov, Alexander M.
AU  - Bondžić, Bojan P.
PY  - 2020
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8806
AB  - Three coordination compounds featuring different types of tetracopper(II) cores, namely [O ⊂ Cu4N(CH2CH2O)34(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. © 2020 Elsevier Inc.
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 M. and Senćanski, Milan V. and Vujačić Nikezić, Ana V. and Kirillova, Marina V. and André, Vania and Kirillov, Alexander M. and Bondžić, Bojan P.",
year = "2020",
abstract = "Three coordination compounds featuring different types of tetracopper(II) cores, namely [O ⊂ Cu4N(CH2CH2O)34(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. © 2020 Elsevier Inc.",
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. M., Senćanski, M. V., Vujačić Nikezić, A. V., Kirillova, M. V., André, V., Kirillov, A. M.,& Bondžić, B. P.. (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, 205, 110990.
https://doi.org/10.1016/j.jinorgbio.2019.110990

Bondžić AM, Senćanski MV, Vujačić Nikezić AV, Kirillova MV, André V, Kirillov AM, Bondžić BP. 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 M., Senćanski, Milan V., Vujačić Nikezić, Ana V., Kirillova, Marina V., André, Vania, Kirillov, Alexander M., Bondžić, Bojan P., "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  - CONF
AU  - Bondžić, Aleksandra M.
AU  - Vujačić Nikezić, Ana V.
AU  - Kirillov, Alexander M.
AU  - Bondžić, Bojan P.
PY  - 2020
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12511
C3  - Fourth WG Meeting CA15135 : Final status of WG activities within MuTaLig COST Action : Book of Abstracts
T1  - Aminoalcoholate-driven tetracopper(II) cores as inhibitors of aggregation of β-amyloid
SP  - 56
EP  - 56
UR  - https://hdl.handle.net/21.15107/rcub_vinar_12511
ER  - 

@conference{
author = "Bondžić, Aleksandra M. and Vujačić Nikezić, Ana V. and Kirillov, Alexander M. and Bondžić, Bojan P.",
year = "2020",
journal = "Fourth WG Meeting CA15135 : Final status of WG activities within MuTaLig COST Action : Book of Abstracts",
title = "Aminoalcoholate-driven tetracopper(II) cores as inhibitors of aggregation of β-amyloid",
pages = "56-56",
url = "https://hdl.handle.net/21.15107/rcub_vinar_12511"
}

Bondžić, A. M., Vujačić Nikezić, A. V., Kirillov, A. M.,& Bondžić, B. P.. (2020). Aminoalcoholate-driven tetracopper(II) cores as inhibitors of aggregation of β-amyloid. in Fourth WG Meeting CA15135 : Final status of WG activities within MuTaLig COST Action : Book of Abstracts, 56-56.
https://hdl.handle.net/21.15107/rcub_vinar_12511

Bondžić AM, Vujačić Nikezić AV, Kirillov AM, Bondžić BP. Aminoalcoholate-driven tetracopper(II) cores as inhibitors of aggregation of β-amyloid. in Fourth WG Meeting CA15135 : Final status of WG activities within MuTaLig COST Action : Book of Abstracts. 2020;:56-56.
https://hdl.handle.net/21.15107/rcub_vinar_12511 .

Bondžić, Aleksandra M., Vujačić Nikezić, Ana V., Kirillov, Alexander M., Bondžić, Bojan P., "Aminoalcoholate-driven tetracopper(II) cores as inhibitors of aggregation of β-amyloid" in Fourth WG Meeting CA15135 : Final status of WG activities within MuTaLig COST Action : Book of Abstracts (2020):56-56,
https://hdl.handle.net/21.15107/rcub_vinar_12511 .