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

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

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

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

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

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - 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  - Lazarević-Pašti, Tamara D.
AU  - Momić, Tatjana
AU  - Onjia, Antonije E.
AU  - Vujisić, Ljubodrag V.
AU  - Vasić, Vesna
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3176
AB  - In order to improve the sensitivity of assays for inhibitors of the enzyme acetylcholine esterase (AChE), an effective method was developed for the conversion of the organophosphate pesticides (OPs) diazinon, malathion, chlorpyrifos, azinphos-methyl and phorate into more toxic inhibitors. This was accomplished by converting them from the thio form into their oxo form using the enzyme myeloperoxidase. The oxo forms, which are the only products of conversion, were determined by AChE bioassays, using either the free enzyme, or a flow injection analysis manifold with immobilized AChE and spectrophotometric detection. All modified OPs exhibited inhibitory power at ppb levels and within 10 min. The method is considered to represent an excellent means for improving the sensitivity of assays for determination of OPs.
PB  - Springer Science and Business Media LLC
T2  - Microchimica Acta
T1  - Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods
VL  - 170
IS  - 3-4
SP  - 289
EP  - 297
DO  - 10.1007/s00604-010-0324-2
ER  - 

@article{
author = "Lazarević-Pašti, Tamara D. and Momić, Tatjana and Onjia, Antonije E. and Vujisić, Ljubodrag V. and Vasić, Vesna",
year = "2010",
abstract = "In order to improve the sensitivity of assays for inhibitors of the enzyme acetylcholine esterase (AChE), an effective method was developed for the conversion of the organophosphate pesticides (OPs) diazinon, malathion, chlorpyrifos, azinphos-methyl and phorate into more toxic inhibitors. This was accomplished by converting them from the thio form into their oxo form using the enzyme myeloperoxidase. The oxo forms, which are the only products of conversion, were determined by AChE bioassays, using either the free enzyme, or a flow injection analysis manifold with immobilized AChE and spectrophotometric detection. All modified OPs exhibited inhibitory power at ppb levels and within 10 min. The method is considered to represent an excellent means for improving the sensitivity of assays for determination of OPs.",
publisher = "Springer Science and Business Media LLC",
journal = "Microchimica Acta",
title = "Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods",
volume = "170",
number = "3-4",
pages = "289-297",
doi = "10.1007/s00604-010-0324-2"
}

Lazarević-Pašti, T. D., Momić, T., Onjia, A. E., Vujisić, L. V.,& Vasić, V.. (2010). Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods. in Microchimica Acta
Springer Science and Business Media LLC., 170(3-4), 289-297.
https://doi.org/10.1007/s00604-010-0324-2

Lazarević-Pašti TD, Momić T, Onjia AE, Vujisić LV, Vasić V. Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods. in Microchimica Acta. 2010;170(3-4):289-297.
doi:10.1007/s00604-010-0324-2 .

Lazarević-Pašti, Tamara D., Momić, Tatjana, Onjia, Antonije E., Vujisić, Ljubodrag V., Vasić, Vesna, "Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods" in Microchimica Acta, 170, no. 3-4 (2010):289-297,
https://doi.org/10.1007/s00604-010-0324-2 . .