TY  - JOUR
AU  - Matić, Ivana Z.
AU  - Mraković, Ana
AU  - Rakočević, Zlatko
AU  - Stoiljković, Milovan
AU  - Pavlović, Vladimir B.
AU  - Momić, Tatjana
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11544
AB  - Background: Although luteolin has been confirmed as potent anticancer agent, its potential application as therapeutic is limited by its water solubility. To overcome this shortcoming nanoparticle technology approach was applied. Owing to their proven low toxicity and the possibility to be easily functionalized gold nanoparticles (AuNP) were the nanosystem of choice used in this study. Novel luteolin capped gold nanoparticles (AuNPL) were synthesized and their anticancer effect towards human cervical adenocarcinoma HeLa cells was investigated in vitro. Methods: AuNPL were synthesized by reducing chloroauric acid by trisodium citrate with subsequent addition of luteoline during synthesis and their physicochemical characterization was done. AuNPL cytotoxicity against HeLa, human malignant melanoma A375, and normal human keratinocytes HaCaT cells was tested by MTT cell survival assay, and their IC50 values were determined. The capability of AuNPL to induce cell cycle arrest and apoptosis in HeLa cells were demonstrated by flow cytometry. The antioxidant activity of AuNPL was assessed by DPPH⋅ and ABTS⋅þ scavenging assays. Cytoprotective properties of AuNPL towards HaCaT cells were examined by measuring the physiological and H2O2 induced intracellular reactive oxygen species (ROS) levels using flow cytometry. Also, genotoxicity of AuNPL in HaCaT cells was investigated by the single cell alkaline comet assay. Results: Spherical AuNPL, stable in aqueous solution up to six months at 4 ◦C were obtained in the synthesis. The selectivity in the cytotoxic action of AuNPL on HeLa and A375 cancer cells compared with their cytotoxicity on normal keratinocytes HaCaT was observed. AuNPL exerted their cytotoxic activity against HeLa cells through accumulation of the cells in the subG1 phase of the cell cycle, inducing the apoptotic cell death mediated by the activation of caspase-3 − 8, and − 9. AuNPL antioxidative potential was confirmed by DPPH⋅ and ABTS⋅þ scavenging assays. IC50 concentration of AuNPL exerted cytoprotective effect against HaCaT cells by the significant reduction of the physiological intracellular ROS level. Additionally, AuNPL were shown as more cytoprotective towards HaCaT cells then luteolin due to the more successful elimination of H2O2 induced intracellular ROS. Moreover, nontoxic concentrations of AuNPL did not cause considerable DNA damage of HaCaT cells, indicating low genotoxicity of the nanoparticles.
T2  - Journal of Trace Elements in Medicine and Biology
T1  - Anticancer effect of novel luteolin capped gold nanoparticles selectively cytotoxic towards human cervical adenocarcinoma HeLa cells: An in vitro approach
VL  - 80
SP  - 127286
DO  - 10.1016/j.jtemb.2023.127286
ER  - 

@article{
author = "Matić, Ivana Z. and Mraković, Ana and Rakočević, Zlatko and Stoiljković, Milovan and Pavlović, Vladimir B. and Momić, Tatjana",
year = "2023",
abstract = "Background: Although luteolin has been confirmed as potent anticancer agent, its potential application as therapeutic is limited by its water solubility. To overcome this shortcoming nanoparticle technology approach was applied. Owing to their proven low toxicity and the possibility to be easily functionalized gold nanoparticles (AuNP) were the nanosystem of choice used in this study. Novel luteolin capped gold nanoparticles (AuNPL) were synthesized and their anticancer effect towards human cervical adenocarcinoma HeLa cells was investigated in vitro. Methods: AuNPL were synthesized by reducing chloroauric acid by trisodium citrate with subsequent addition of luteoline during synthesis and their physicochemical characterization was done. AuNPL cytotoxicity against HeLa, human malignant melanoma A375, and normal human keratinocytes HaCaT cells was tested by MTT cell survival assay, and their IC50 values were determined. The capability of AuNPL to induce cell cycle arrest and apoptosis in HeLa cells were demonstrated by flow cytometry. The antioxidant activity of AuNPL was assessed by DPPH⋅ and ABTS⋅þ scavenging assays. Cytoprotective properties of AuNPL towards HaCaT cells were examined by measuring the physiological and H2O2 induced intracellular reactive oxygen species (ROS) levels using flow cytometry. Also, genotoxicity of AuNPL in HaCaT cells was investigated by the single cell alkaline comet assay. Results: Spherical AuNPL, stable in aqueous solution up to six months at 4 ◦C were obtained in the synthesis. The selectivity in the cytotoxic action of AuNPL on HeLa and A375 cancer cells compared with their cytotoxicity on normal keratinocytes HaCaT was observed. AuNPL exerted their cytotoxic activity against HeLa cells through accumulation of the cells in the subG1 phase of the cell cycle, inducing the apoptotic cell death mediated by the activation of caspase-3 − 8, and − 9. AuNPL antioxidative potential was confirmed by DPPH⋅ and ABTS⋅þ scavenging assays. IC50 concentration of AuNPL exerted cytoprotective effect against HaCaT cells by the significant reduction of the physiological intracellular ROS level. Additionally, AuNPL were shown as more cytoprotective towards HaCaT cells then luteolin due to the more successful elimination of H2O2 induced intracellular ROS. Moreover, nontoxic concentrations of AuNPL did not cause considerable DNA damage of HaCaT cells, indicating low genotoxicity of the nanoparticles.",
journal = "Journal of Trace Elements in Medicine and Biology",
title = "Anticancer effect of novel luteolin capped gold nanoparticles selectively cytotoxic towards human cervical adenocarcinoma HeLa cells: An in vitro approach",
volume = "80",
pages = "127286",
doi = "10.1016/j.jtemb.2023.127286"
}

Matić, I. Z., Mraković, A., Rakočević, Z., Stoiljković, M., Pavlović, V. B.,& Momić, T.. (2023). Anticancer effect of novel luteolin capped gold nanoparticles selectively cytotoxic towards human cervical adenocarcinoma HeLa cells: An in vitro approach. in Journal of Trace Elements in Medicine and Biology, 80, 127286.
https://doi.org/10.1016/j.jtemb.2023.127286

Matić IZ, Mraković A, Rakočević Z, Stoiljković M, Pavlović VB, Momić T. Anticancer effect of novel luteolin capped gold nanoparticles selectively cytotoxic towards human cervical adenocarcinoma HeLa cells: An in vitro approach. in Journal of Trace Elements in Medicine and Biology. 2023;80:127286.
doi:10.1016/j.jtemb.2023.127286 .

Matić, Ivana Z., Mraković, Ana, Rakočević, Zlatko, Stoiljković, Milovan, Pavlović, Vladimir B., Momić, Tatjana, "Anticancer effect of novel luteolin capped gold nanoparticles selectively cytotoxic towards human cervical adenocarcinoma HeLa cells: An in vitro approach" in Journal of Trace Elements in Medicine and Biology, 80 (2023):127286,
https://doi.org/10.1016/j.jtemb.2023.127286 . .

TY  - CONF
AU  - Filipović Tričković, Jelena G.
AU  - Kokunešoski, Maja
AU  - Momić, Tatjana
AU  - Jovanović, Ivan G.
AU  - Anastasov, Marina
AU  - Stojanović, Dragana
AU  - Valenta Šobot, Ana
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11409
C3  - 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book
T1  - Toxicity assessment of mesoporous silica nanoparticles under different extraction procedures
T1  - Procena toksičnosti mezoporoznih nanočestica silicijum dioksida pri različitim postupcima ekstrakcije
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11409
ER  - 

@conference{
author = "Filipović Tričković, Jelena G. and Kokunešoski, Maja and Momić, Tatjana and Jovanović, Ivan G. and Anastasov, Marina and Stojanović, Dragana and Valenta Šobot, Ana",
year = "2023",
journal = "13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book",
title = "Toxicity assessment of mesoporous silica nanoparticles under different extraction procedures, Procena toksičnosti mezoporoznih nanočestica silicijum dioksida pri različitim postupcima ekstrakcije",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11409"
}

Filipović Tričković, J. G., Kokunešoski, M., Momić, T., Jovanović, I. G., Anastasov, M., Stojanović, D.,& Valenta Šobot, A.. (2023). Toxicity assessment of mesoporous silica nanoparticles under different extraction procedures. in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book.
https://hdl.handle.net/21.15107/rcub_vinar_11409

Filipović Tričković JG, Kokunešoski M, Momić T, Jovanović IG, Anastasov M, Stojanović D, Valenta Šobot A. Toxicity assessment of mesoporous silica nanoparticles under different extraction procedures. in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book. 2023;.
https://hdl.handle.net/21.15107/rcub_vinar_11409 .

Filipović Tričković, Jelena G., Kokunešoski, Maja, Momić, Tatjana, Jovanović, Ivan G., Anastasov, Marina, Stojanović, Dragana, Valenta Šobot, Ana, "Toxicity assessment of mesoporous silica nanoparticles under different extraction procedures" in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book (2023),
https://hdl.handle.net/21.15107/rcub_vinar_11409 .

TY  - CONF
AU  - Valenta Šobot, Ana
AU  - Drakulić, Dunja
AU  - Kokunešoski, Maja
AU  - Momić, Tatjana
AU  - Filipović Tričković, Jelena G.
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11410
C3  - 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book
T1  - Loganic acid induces apoptosis in human peripheral blood mononuclear cells
T1  - Loganska kiselina indukuje apoptozu u mononuklearnim ćelijama periferne krvi čoveka
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11410
ER  - 

@conference{
author = "Valenta Šobot, Ana and Drakulić, Dunja and Kokunešoski, Maja and Momić, Tatjana and Filipović Tričković, Jelena G.",
year = "2023",
journal = "13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book",
title = "Loganic acid induces apoptosis in human peripheral blood mononuclear cells, Loganska kiselina indukuje apoptozu u mononuklearnim ćelijama periferne krvi čoveka",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11410"
}

Valenta Šobot, A., Drakulić, D., Kokunešoski, M., Momić, T.,& Filipović Tričković, J. G.. (2023). Loganic acid induces apoptosis in human peripheral blood mononuclear cells. in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book.
https://hdl.handle.net/21.15107/rcub_vinar_11410

Valenta Šobot A, Drakulić D, Kokunešoski M, Momić T, Filipović Tričković JG. Loganic acid induces apoptosis in human peripheral blood mononuclear cells. in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book. 2023;.
https://hdl.handle.net/21.15107/rcub_vinar_11410 .

Valenta Šobot, Ana, Drakulić, Dunja, Kokunešoski, Maja, Momić, Tatjana, Filipović Tričković, Jelena G., "Loganic acid induces apoptosis in human peripheral blood mononuclear cells" in 13th international congress of the Serbian society of toxicology & 1st toxSEE regional conference : abstract book (2023),
https://hdl.handle.net/21.15107/rcub_vinar_11410 .

TY  - CONF
AU  - Valenta Šobot, Ana
AU  - Filipović Tričković, Jelena
AU  - Drakulić, Dunja
AU  - Leskovac, Andreja
AU  - Petrović, Sandra
AU  - Momić, Tatjana
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11582
AB  - Sweroside (Sw) is a secondary metabolite commonly found in plants belonging to the Gentianaceae family [1]. This iridoid compound is well-known for its anti-inflammatory [2], antidiabetic [3] and antitumor properties [4], which have been studied in pathological model systems. In transformed cell lines, Sw displays an antitumor effect by apoptosis activation [5]. Since healthy cells are also exposed to cancer therapy applied in vivo, our goal was to determine Sw’s cytotoxic concentration in primary human peripheral blood mononuclear cells (PBMCs) after 48 h of treatment with a range of concentration from 20 μM to 130 μM Sw in vitro, and to analyze whether the cytotoxic effect was due to activated apoptosis. According to the obtained results of the trypan blue dye exclusion test, 48 h of treatment with 50 μM Sw and higher concentrations led to a significant decrease in cell number. The DNA fragmentation assay indicated that following 50 μM Sw treatment, cells are dying in an apoptosis-like manner since the level of DNA fragments was 3.5 times higher than in the untreated control. The type of cell death was confirmed by immunoblot analysis of apoptosis- specific protein markers, which revealed the elevation of cleaved caspase-3 and PARP1 89 kDa fragments. Our findings showed that like in transformed cell lines, Sw in healthy cells can also activate apoptosis. A potential difference in sensitivity to Sw treatment between healthy and transformed cells could justify Sw treatment in anticancer therapy.
PB  - Belgrade : University of Belgrade, Faculty of Agriculture
C3  - 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts
T1  - Sweroside displays a cytotoxic effect by activating apoptosis in human peripheral blood mononuclear cells
SP  - 47
EP  - 47
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11582
ER  - 

@conference{
author = "Valenta Šobot, Ana and Filipović Tričković, Jelena and Drakulić, Dunja and Leskovac, Andreja and Petrović, Sandra and Momić, Tatjana",
year = "2022",
abstract = "Sweroside (Sw) is a secondary metabolite commonly found in plants belonging to the Gentianaceae family [1]. This iridoid compound is well-known for its anti-inflammatory [2], antidiabetic [3] and antitumor properties [4], which have been studied in pathological model systems. In transformed cell lines, Sw displays an antitumor effect by apoptosis activation [5]. Since healthy cells are also exposed to cancer therapy applied in vivo, our goal was to determine Sw’s cytotoxic concentration in primary human peripheral blood mononuclear cells (PBMCs) after 48 h of treatment with a range of concentration from 20 μM to 130 μM Sw in vitro, and to analyze whether the cytotoxic effect was due to activated apoptosis. According to the obtained results of the trypan blue dye exclusion test, 48 h of treatment with 50 μM Sw and higher concentrations led to a significant decrease in cell number. The DNA fragmentation assay indicated that following 50 μM Sw treatment, cells are dying in an apoptosis-like manner since the level of DNA fragments was 3.5 times higher than in the untreated control. The type of cell death was confirmed by immunoblot analysis of apoptosis- specific protein markers, which revealed the elevation of cleaved caspase-3 and PARP1 89 kDa fragments. Our findings showed that like in transformed cell lines, Sw in healthy cells can also activate apoptosis. A potential difference in sensitivity to Sw treatment between healthy and transformed cells could justify Sw treatment in anticancer therapy.",
publisher = "Belgrade : University of Belgrade, Faculty of Agriculture",
journal = "1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts",
title = "Sweroside displays a cytotoxic effect by activating apoptosis in human peripheral blood mononuclear cells",
pages = "47-47",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11582"
}

Valenta Šobot, A., Filipović Tričković, J., Drakulić, D., Leskovac, A., Petrović, S.,& Momić, T.. (2022). Sweroside displays a cytotoxic effect by activating apoptosis in human peripheral blood mononuclear cells. in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts
Belgrade : University of Belgrade, Faculty of Agriculture., 47-47.
https://hdl.handle.net/21.15107/rcub_vinar_11582

Valenta Šobot A, Filipović Tričković J, Drakulić D, Leskovac A, Petrović S, Momić T. Sweroside displays a cytotoxic effect by activating apoptosis in human peripheral blood mononuclear cells. in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts. 2022;:47-47.
https://hdl.handle.net/21.15107/rcub_vinar_11582 .

Valenta Šobot, Ana, Filipović Tričković, Jelena, Drakulić, Dunja, Leskovac, Andreja, Petrović, Sandra, Momić, Tatjana, "Sweroside displays a cytotoxic effect by activating apoptosis in human peripheral blood mononuclear cells" in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts (2022):47-47,
https://hdl.handle.net/21.15107/rcub_vinar_11582 .

TY  - CONF
AU  - Valenta Šobot, Ana
AU  - Filipović Tričković, Jelena
AU  - Leskovac, Andreja
AU  - Petrović, Sandra
AU  - Momić, Tatjana
PY  - 2022
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/11583
AB  - Quercetin (Q) is one of the most common and well researched antioxidant flavonoids, which usually occurs in plant-based foods, and medicinal plants. It was shown that quercetin exerts many beneficial effects on human health, including prevention of cancer and heart diseases. Quercetin was found to be toxic toward various types of cancer cell, still, at higher concentrations it was also shown toxic toward normal human cells [1,2]. One of the approaches to overcome this shortcoming offers nanotechnology which enables the novel perspective of phytochemical usage in contemporary medicine [3]. The strategy of binding quercetin to the gold nanoparticles during their synthesis was used, which resulted in quercetin capped gold nanoparticles (NPQ) [4]. Trypan blue exclusion test [5] was used to evaluate peripheral blood mononuclear cells (PBMC) viability after their exposure to either NPQ or free Q during 24, 48 and 72 h, at 37 °C, in the range of quercetin concentrations from 5 to 50 μg/mL. A significant reduction in the cell count was observed in PBMC cultures treated with 10, 20, and 50 μg/mL of free Q, for all exposure times. The treatments of increasing concentrations and exposure times lowered the cells viability, resulting in 63% of the viable cells, following 72 h of the treatment with 50 μg/mL of free Q. Although NPQ treatments affected the cells viability in a concentration- and time-dependent manner the treatment with 50 μg/mL of NPQ for 72 h, had a milder effect on PBMC cultures than free Q, resulting in 81% of the viable cells (Figure 1). According to the obtained results, NPQ were shown less toxic toward PBMC than free Q.
PB  - Belgrade : University of Belgrade, Faculty of Agriculture
C3  - 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts
T1  - Nanotechnology approach for diminishing quercetin toxicity toward peripheral blood mononuclear cells
SP  - 64
EP  - 64
UR  - https://hdl.handle.net/21.15107/rcub_vinar_11583
ER  - 

@conference{
author = "Valenta Šobot, Ana and Filipović Tričković, Jelena and Leskovac, Andreja and Petrović, Sandra and Momić, Tatjana",
year = "2022",
abstract = "Quercetin (Q) is one of the most common and well researched antioxidant flavonoids, which usually occurs in plant-based foods, and medicinal plants. It was shown that quercetin exerts many beneficial effects on human health, including prevention of cancer and heart diseases. Quercetin was found to be toxic toward various types of cancer cell, still, at higher concentrations it was also shown toxic toward normal human cells [1,2]. One of the approaches to overcome this shortcoming offers nanotechnology which enables the novel perspective of phytochemical usage in contemporary medicine [3]. The strategy of binding quercetin to the gold nanoparticles during their synthesis was used, which resulted in quercetin capped gold nanoparticles (NPQ) [4]. Trypan blue exclusion test [5] was used to evaluate peripheral blood mononuclear cells (PBMC) viability after their exposure to either NPQ or free Q during 24, 48 and 72 h, at 37 °C, in the range of quercetin concentrations from 5 to 50 μg/mL. A significant reduction in the cell count was observed in PBMC cultures treated with 10, 20, and 50 μg/mL of free Q, for all exposure times. The treatments of increasing concentrations and exposure times lowered the cells viability, resulting in 63% of the viable cells, following 72 h of the treatment with 50 μg/mL of free Q. Although NPQ treatments affected the cells viability in a concentration- and time-dependent manner the treatment with 50 μg/mL of NPQ for 72 h, had a milder effect on PBMC cultures than free Q, resulting in 81% of the viable cells (Figure 1). According to the obtained results, NPQ were shown less toxic toward PBMC than free Q.",
publisher = "Belgrade : University of Belgrade, Faculty of Agriculture",
journal = "1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts",
title = "Nanotechnology approach for diminishing quercetin toxicity toward peripheral blood mononuclear cells",
pages = "64-64",
url = "https://hdl.handle.net/21.15107/rcub_vinar_11583"
}

Valenta Šobot, A., Filipović Tričković, J., Leskovac, A., Petrović, S.,& Momić, T.. (2022). Nanotechnology approach for diminishing quercetin toxicity toward peripheral blood mononuclear cells. in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts
Belgrade : University of Belgrade, Faculty of Agriculture., 64-64.
https://hdl.handle.net/21.15107/rcub_vinar_11583

Valenta Šobot A, Filipović Tričković J, Leskovac A, Petrović S, Momić T. Nanotechnology approach for diminishing quercetin toxicity toward peripheral blood mononuclear cells. in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts. 2022;:64-64.
https://hdl.handle.net/21.15107/rcub_vinar_11583 .

Valenta Šobot, Ana, Filipović Tričković, Jelena, Leskovac, Andreja, Petrović, Sandra, Momić, Tatjana, "Nanotechnology approach for diminishing quercetin toxicity toward peripheral blood mononuclear cells" in 1-EuSPMF - 1st European symposium on phytochemicals in medicine and food : Book of abstracts (2022):64-64,
https://hdl.handle.net/21.15107/rcub_vinar_11583 .

TY  - CONF
AU  - Nemoda, Milica
AU  - Pavlović, M.
AU  - Stoiljković, Milovan
AU  - Momić, Tatjana
PY  - 2021
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12522
AB  - We report on the use of gold nanoparticles (AuNPs) as a colorimetric probe for quercetin (Q). The method is based on the aggregation of the AuNPs that is caused by various quercetin concentrations in the range of 4 mg/L - 15 mg/L and leads to a visually detectable color change. Concentration-dependent aggregation is confirmed by recording of UV-visible absorption spectra. The method provides a useful tool for the rapid visual quercetin determination.
PB  - Belgrade : Vinča Institute of Nuclear Sciences - National Institute of the Republic of Serbia
C3  - Proceedings / 7th Workshop Specific Methods for Food Safety and Quality, September 22nd, 2021, Belgrade, Serbia [is an online satellite event of] 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry - Physical Chemistry 2021
T1  - Visual detection of quercetin using gold nanoparticles
SP  - 28
EP  - 31
UR  - https://hdl.handle.net/21.15107/rcub_vinar_12522
ER  - 

@conference{
author = "Nemoda, Milica and Pavlović, M. and Stoiljković, Milovan and Momić, Tatjana",
year = "2021",
abstract = "We report on the use of gold nanoparticles (AuNPs) as a colorimetric probe for quercetin (Q). The method is based on the aggregation of the AuNPs that is caused by various quercetin concentrations in the range of 4 mg/L - 15 mg/L and leads to a visually detectable color change. Concentration-dependent aggregation is confirmed by recording of UV-visible absorption spectra. The method provides a useful tool for the rapid visual quercetin determination.",
publisher = "Belgrade : Vinča Institute of Nuclear Sciences - National Institute of the Republic of Serbia",
journal = "Proceedings / 7th Workshop Specific Methods for Food Safety and Quality, September 22nd, 2021, Belgrade, Serbia [is an online satellite event of] 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry - Physical Chemistry 2021",
title = "Visual detection of quercetin using gold nanoparticles",
pages = "28-31",
url = "https://hdl.handle.net/21.15107/rcub_vinar_12522"
}

Nemoda, M., Pavlović, M., Stoiljković, M.,& Momić, T.. (2021). Visual detection of quercetin using gold nanoparticles. in Proceedings / 7th Workshop Specific Methods for Food Safety and Quality, September 22nd, 2021, Belgrade, Serbia [is an online satellite event of] 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry - Physical Chemistry 2021
Belgrade : Vinča Institute of Nuclear Sciences - National Institute of the Republic of Serbia., 28-31.
https://hdl.handle.net/21.15107/rcub_vinar_12522

Nemoda M, Pavlović M, Stoiljković M, Momić T. Visual detection of quercetin using gold nanoparticles. in Proceedings / 7th Workshop Specific Methods for Food Safety and Quality, September 22nd, 2021, Belgrade, Serbia [is an online satellite event of] 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry - Physical Chemistry 2021. 2021;:28-31.
https://hdl.handle.net/21.15107/rcub_vinar_12522 .

Nemoda, Milica, Pavlović, M., Stoiljković, Milovan, Momić, Tatjana, "Visual detection of quercetin using gold nanoparticles" in Proceedings / 7th Workshop Specific Methods for Food Safety and Quality, September 22nd, 2021, Belgrade, Serbia [is an online satellite event of] 15th International Conference on Fundamental and Applied Aspects of Physical Chemistry - Physical Chemistry 2021 (2021):28-31,
https://hdl.handle.net/21.15107/rcub_vinar_12522 .

TY  - JOUR
AU  - Vujačić Nikezić, Ana V.
AU  - Janjić, Goran V.
AU  - Bondžić, Aleksandra M.
AU  - Zarić, Božidarka
AU  - Vasić Anićijević, Dragana D.
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2018
UR  - http://xlink.rsc.org/?DOI=C8MT00111A
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/7812
AB  - The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4]-, [AuCl2(dmso)2]+, [AuCl2(bipy)]+) and Pt(ii) ([PtCl2(dmso)2]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4]- and [PtCl2(dmso)2] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.
T2  - Metallomics
T1  - Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites
VL  - 10
IS  - 7
SP  - 1003
EP  - 1015
DO  - 10.1039/C8MT00111A
ER  - 

@article{
author = "Vujačić Nikezić, Ana V. and Janjić, Goran V. and Bondžić, Aleksandra M. and Zarić, Božidarka and Vasić Anićijević, Dragana D. and Momić, Tatjana and Vasić, Vesna M.",
year = "2018",
abstract = "The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4]-, [AuCl2(dmso)2]+, [AuCl2(bipy)]+) and Pt(ii) ([PtCl2(dmso)2]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4]- and [PtCl2(dmso)2] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.",
journal = "Metallomics",
title = "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites",
volume = "10",
number = "7",
pages = "1003-1015",
doi = "10.1039/C8MT00111A"
}

Vujačić Nikezić, A. V., Janjić, G. V., Bondžić, A. M., Zarić, B., Vasić Anićijević, D. D., Momić, T.,& Vasić, V. M.. (2018). Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics, 10(7), 1003-1015.
https://doi.org/10.1039/C8MT00111A

Vujačić Nikezić AV, Janjić GV, Bondžić AM, Zarić B, Vasić Anićijević DD, Momić T, Vasić VM. Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics. 2018;10(7):1003-1015.
doi:10.1039/C8MT00111A .

Vujačić Nikezić, Ana V., Janjić, Goran V., Bondžić, Aleksandra M., Zarić, Božidarka, Vasić Anićijević, Dragana D., Momić, Tatjana, Vasić, Vesna M., "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites" in Metallomics, 10, no. 7 (2018):1003-1015,
https://doi.org/10.1039/C8MT00111A . .

TY  - JOUR
AU  - Lazarević-Pašti, Tamara
AU  - Leskovac, Andreja
AU  - Momić, Tatjana
AU  - Petrović, Sandra
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1796
AB  - Background: Acetylcholinesterase (AChE) is involved in the termination of impulse transmission by rapid hydrolysis of the neurotransmitter acetylcholine in numerous cholinergic pathways in the central and peripheral nervous systems. The enzyme inactivation leads to acetylcholine accumulation, hyperstimulation of nicotinic and muscarinic receptors, and disrupted neurotransmission. Hence, acetylcholinesterase inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs for different neurodegenerative diseases (such as Alzheimers and Parkinsons) as well as toxins. At the same time, there are increasing evidence that in non-neuronal context, AChE is involved in the regulation of cell proliferation, differentiation, apoptosis and cell-cell interaction. An irregular expression of AChE has been found in different types of tumors, suggesting the involvement of AChE in the regulation of tumor development. Having all this in mind, there is a possibility that some AChE inhibitors could be used as anti-cancer agents. Objective: This contribution will discuss a broad range of possible application of different AChE inhibitors as drugs, from well-known anti-Alzheimers disease drugs to their use in cancer treatment in future. Emphasis will be put on various known AChE inhibitors classes, whose application as drugs could be controversy, as well as on newly investigated natural products, which can also modulate AChE activity. Conclusion: It is not clear a patient treated for neurodegenerative condition prone to increased risk for some types of cancer and vice versa. This is necessary to keep in mind during rational drug design process for all therapies, which are based on AChE as a target molecule.
T2  - Current Medicinal Chemistry
T1  - Modulators of Acetylcholinesterase Activity: From Alzheimers Disease to Anti-Cancer Drugs
VL  - 24
IS  - 30
SP  - 3283
EP  - 3309
DO  - 10.2174/0929867324666170705123509
ER  - 

@article{
author = "Lazarević-Pašti, Tamara and Leskovac, Andreja and Momić, Tatjana and Petrović, Sandra and Vasić, Vesna M.",
year = "2017",
abstract = "Background: Acetylcholinesterase (AChE) is involved in the termination of impulse transmission by rapid hydrolysis of the neurotransmitter acetylcholine in numerous cholinergic pathways in the central and peripheral nervous systems. The enzyme inactivation leads to acetylcholine accumulation, hyperstimulation of nicotinic and muscarinic receptors, and disrupted neurotransmission. Hence, acetylcholinesterase inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs for different neurodegenerative diseases (such as Alzheimers and Parkinsons) as well as toxins. At the same time, there are increasing evidence that in non-neuronal context, AChE is involved in the regulation of cell proliferation, differentiation, apoptosis and cell-cell interaction. An irregular expression of AChE has been found in different types of tumors, suggesting the involvement of AChE in the regulation of tumor development. Having all this in mind, there is a possibility that some AChE inhibitors could be used as anti-cancer agents. Objective: This contribution will discuss a broad range of possible application of different AChE inhibitors as drugs, from well-known anti-Alzheimers disease drugs to their use in cancer treatment in future. Emphasis will be put on various known AChE inhibitors classes, whose application as drugs could be controversy, as well as on newly investigated natural products, which can also modulate AChE activity. Conclusion: It is not clear a patient treated for neurodegenerative condition prone to increased risk for some types of cancer and vice versa. This is necessary to keep in mind during rational drug design process for all therapies, which are based on AChE as a target molecule.",
journal = "Current Medicinal Chemistry",
title = "Modulators of Acetylcholinesterase Activity: From Alzheimers Disease to Anti-Cancer Drugs",
volume = "24",
number = "30",
pages = "3283-3309",
doi = "10.2174/0929867324666170705123509"
}

Lazarević-Pašti, T., Leskovac, A., Momić, T., Petrović, S.,& Vasić, V. M.. (2017). Modulators of Acetylcholinesterase Activity: From Alzheimers Disease to Anti-Cancer Drugs. in Current Medicinal Chemistry, 24(30), 3283-3309.
https://doi.org/10.2174/0929867324666170705123509

Lazarević-Pašti T, Leskovac A, Momić T, Petrović S, Vasić VM. Modulators of Acetylcholinesterase Activity: From Alzheimers Disease to Anti-Cancer Drugs. in Current Medicinal Chemistry. 2017;24(30):3283-3309.
doi:10.2174/0929867324666170705123509 .

Lazarević-Pašti, Tamara, Leskovac, Andreja, Momić, Tatjana, Petrović, Sandra, Vasić, Vesna M., "Modulators of Acetylcholinesterase Activity: From Alzheimers Disease to Anti-Cancer Drugs" in Current Medicinal Chemistry, 24, no. 30 (2017):3283-3309,
https://doi.org/10.2174/0929867324666170705123509 . .

TY  - JOUR
AU  - Momić, Tatjana
AU  - Lazarević-Pašti, Tamara
AU  - Bogdanović, Una
AU  - Vodnik, Vesna
AU  - Mraković, Ana Đ.
AU  - Rakočević, Zlatko Lj.
AU  - Pavlović, Vladimir B.
AU  - Vasić, Vesna M.
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1347
AB  - Organophosphorus pesticide dimethoate was adsorbed onto gold nanospheres and nanorods in aqueous solution using batch technique. Adsorption of dimethoate onto gold nanoparticles was confirmed by UV-Vis spectrophotometry, TEM, AFM, and FTIR analysis. The adsorption of nanospheres resulted in aggregation which was not the case with nanorods. Nanoparticles adsorption features were characterized using Langmuir and Freundlich isotherm models. The Langmuir adsorption isotherm was found to have the best fit to the experimental data for both types of nanoparticles. Adsorption capacity detected for nanospheres is 456 mg/g and for nanorods is 57.1 mg/g. Also, nanoparticles were successfully used for dimethoate removal from spiked drinking water while nanospheres were shown to be more efficient than nanorods.
T2  - Journal of Nanomaterials
T1  - Adsorption of Organophosphate Pesticide Dimethoate on Gold Nanospheres and Nanorods
DO  - 10.1155/2016/8910271
ER  - 

@article{
author = "Momić, Tatjana and Lazarević-Pašti, Tamara and Bogdanović, Una and Vodnik, Vesna and Mraković, Ana Đ. and Rakočević, Zlatko Lj. and Pavlović, Vladimir B. and Vasić, Vesna M.",
year = "2016",
abstract = "Organophosphorus pesticide dimethoate was adsorbed onto gold nanospheres and nanorods in aqueous solution using batch technique. Adsorption of dimethoate onto gold nanoparticles was confirmed by UV-Vis spectrophotometry, TEM, AFM, and FTIR analysis. The adsorption of nanospheres resulted in aggregation which was not the case with nanorods. Nanoparticles adsorption features were characterized using Langmuir and Freundlich isotherm models. The Langmuir adsorption isotherm was found to have the best fit to the experimental data for both types of nanoparticles. Adsorption capacity detected for nanospheres is 456 mg/g and for nanorods is 57.1 mg/g. Also, nanoparticles were successfully used for dimethoate removal from spiked drinking water while nanospheres were shown to be more efficient than nanorods.",
journal = "Journal of Nanomaterials",
title = "Adsorption of Organophosphate Pesticide Dimethoate on Gold Nanospheres and Nanorods",
doi = "10.1155/2016/8910271"
}

Momić, T., Lazarević-Pašti, T., Bogdanović, U., Vodnik, V., Mraković, A. Đ., Rakočević, Z. Lj., Pavlović, V. B.,& Vasić, V. M.. (2016). Adsorption of Organophosphate Pesticide Dimethoate on Gold Nanospheres and Nanorods. in Journal of Nanomaterials.
https://doi.org/10.1155/2016/8910271

Momić T, Lazarević-Pašti T, Bogdanović U, Vodnik V, Mraković AĐ, Rakočević ZL, Pavlović VB, Vasić VM. Adsorption of Organophosphate Pesticide Dimethoate on Gold Nanospheres and Nanorods. in Journal of Nanomaterials. 2016;.
doi:10.1155/2016/8910271 .

Momić, Tatjana, Lazarević-Pašti, Tamara, Bogdanović, Una, Vodnik, Vesna, Mraković, Ana Đ., Rakočević, Zlatko Lj., Pavlović, Vladimir B., Vasić, Vesna M., "Adsorption of Organophosphate Pesticide Dimethoate on Gold Nanospheres and Nanorods" in Journal of Nanomaterials (2016),
https://doi.org/10.1155/2016/8910271 . .

TY  - JOUR
AU  - Lazarević-Pašti, Tamara
AU  - Momić, Tatjana
AU  - Radojevic, Milos M.
AU  - Vasić, Vesna M.
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5650
AB  - Inhibitory effects of five organophosphorus pesticides (diazinon, malathion, chlorpyrifos, azinphosmethyl and phorate) and their oxo-analogs on human myeloperoxidase (MPO) activity were investigated. While inspecting separately peroxidase and chlorination activity, it was observed that investigated OPs affect peroxidase activity, but not chlorination activity. Among investigated pesticides, malathion and malaoxon have showed the highest power to inhibit MPO peroxidase activity With IC50 values of the order of 3 x 10(-7) and 5 x 10(-9) M, respectively. It was proposed that inhibition trend is rendered by molecular structure which invokes steric hindrance for OPs interaction with MPO active center responsible for peroxidase activity. In addition, it was concluded that physiological function of MPO is not affected by any of the investigated OPs. (C) 2013 Elsevier Inc. All rights reserved.
T2  - Pesticide Biochemistry and Physiology
T1  - Influence of organophosphorus pesticides on peroxidase and chlorination activity of human myeloperoxidase
VL  - 107
IS  - 1
SP  - 55
EP  - 60
DO  - 10.1016/j.pestbp.2013.05.004
ER  - 

@article{
author = "Lazarević-Pašti, Tamara and Momić, Tatjana and Radojevic, Milos M. and Vasić, Vesna M.",
year = "2013",
abstract = "Inhibitory effects of five organophosphorus pesticides (diazinon, malathion, chlorpyrifos, azinphosmethyl and phorate) and their oxo-analogs on human myeloperoxidase (MPO) activity were investigated. While inspecting separately peroxidase and chlorination activity, it was observed that investigated OPs affect peroxidase activity, but not chlorination activity. Among investigated pesticides, malathion and malaoxon have showed the highest power to inhibit MPO peroxidase activity With IC50 values of the order of 3 x 10(-7) and 5 x 10(-9) M, respectively. It was proposed that inhibition trend is rendered by molecular structure which invokes steric hindrance for OPs interaction with MPO active center responsible for peroxidase activity. In addition, it was concluded that physiological function of MPO is not affected by any of the investigated OPs. (C) 2013 Elsevier Inc. All rights reserved.",
journal = "Pesticide Biochemistry and Physiology",
title = "Influence of organophosphorus pesticides on peroxidase and chlorination activity of human myeloperoxidase",
volume = "107",
number = "1",
pages = "55-60",
doi = "10.1016/j.pestbp.2013.05.004"
}

Lazarević-Pašti, T., Momić, T., Radojevic, M. M.,& Vasić, V. M.. (2013). Influence of organophosphorus pesticides on peroxidase and chlorination activity of human myeloperoxidase. in Pesticide Biochemistry and Physiology, 107(1), 55-60.
https://doi.org/10.1016/j.pestbp.2013.05.004

Lazarević-Pašti T, Momić T, Radojevic MM, Vasić VM. Influence of organophosphorus pesticides on peroxidase and chlorination activity of human myeloperoxidase. in Pesticide Biochemistry and Physiology. 2013;107(1):55-60.
doi:10.1016/j.pestbp.2013.05.004 .

Lazarević-Pašti, Tamara, Momić, Tatjana, Radojevic, Milos M., Vasić, Vesna M., "Influence of organophosphorus pesticides on peroxidase and chlorination activity of human myeloperoxidase" in Pesticide Biochemistry and Physiology, 107, no. 1 (2013):55-60,
https://doi.org/10.1016/j.pestbp.2013.05.004 . .

TY  - JOUR
AU  - Lazarević-Pašti, Tamara
AU  - Čolović, Mirjana B.
AU  - Savić, Jasmina
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2011
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4332
AB  - The aim of the work was to investigate the in vitro oxidation of diazinon and malathion, organophosphorous pesticides (OPs) containing phosphorthioate group, catalyzed by enzyme myeloperoxidase (MPO). The oxidation was performed in the presence of hydrogen peroxide. The products were identified as oxon derivatives (phosphates), where the sulfur atom from thioate group was substituted by an oxygen atom. No hydrolysis products were detected after enzyme - induced oxidation. The oxidation efficiency was controlled using acethylcholinesterase (AChE) bioassay for determination of oxon derivatives concentration. The influence of OPs concentration, incubation time of OPs with MPO, as well as MPO concentration on the yield of oxo forms was investigated. Kinetic constants of MPO in oxidation of malathion and diazinon were estimated. The maximum concentration of oxo forms was achieved after 10 min incubation of OPs in 50 mM phosphate buffer (pH 6.0) with 100 nM MPO. (C) 2011 Elsevier Inc. All rights reserved.
T2  - Pesticide Biochemistry and Physiology
T1  - Oxidation of diazinon and malathion by myeloperoxidase
VL  - 100
IS  - 2
SP  - 140
EP  - 144
DO  - 10.1016/j.pestbp.2011.03.001
ER  - 

@article{
author = "Lazarević-Pašti, Tamara and Čolović, Mirjana B. and Savić, Jasmina and Momić, Tatjana and Vasić, Vesna M.",
year = "2011",
abstract = "The aim of the work was to investigate the in vitro oxidation of diazinon and malathion, organophosphorous pesticides (OPs) containing phosphorthioate group, catalyzed by enzyme myeloperoxidase (MPO). The oxidation was performed in the presence of hydrogen peroxide. The products were identified as oxon derivatives (phosphates), where the sulfur atom from thioate group was substituted by an oxygen atom. No hydrolysis products were detected after enzyme - induced oxidation. The oxidation efficiency was controlled using acethylcholinesterase (AChE) bioassay for determination of oxon derivatives concentration. The influence of OPs concentration, incubation time of OPs with MPO, as well as MPO concentration on the yield of oxo forms was investigated. Kinetic constants of MPO in oxidation of malathion and diazinon were estimated. The maximum concentration of oxo forms was achieved after 10 min incubation of OPs in 50 mM phosphate buffer (pH 6.0) with 100 nM MPO. (C) 2011 Elsevier Inc. All rights reserved.",
journal = "Pesticide Biochemistry and Physiology",
title = "Oxidation of diazinon and malathion by myeloperoxidase",
volume = "100",
number = "2",
pages = "140-144",
doi = "10.1016/j.pestbp.2011.03.001"
}

Lazarević-Pašti, T., Čolović, M. B., Savić, J., Momić, T.,& Vasić, V. M.. (2011). Oxidation of diazinon and malathion by myeloperoxidase. in Pesticide Biochemistry and Physiology, 100(2), 140-144.
https://doi.org/10.1016/j.pestbp.2011.03.001

Lazarević-Pašti T, Čolović MB, Savić J, Momić T, Vasić VM. Oxidation of diazinon and malathion by myeloperoxidase. in Pesticide Biochemistry and Physiology. 2011;100(2):140-144.
doi:10.1016/j.pestbp.2011.03.001 .

Lazarević-Pašti, Tamara, Čolović, Mirjana B., Savić, Jasmina, Momić, Tatjana, Vasić, Vesna M., "Oxidation of diazinon and malathion by myeloperoxidase" in Pesticide Biochemistry and Physiology, 100, no. 2 (2011):140-144,
https://doi.org/10.1016/j.pestbp.2011.03.001 . .

TY  - CONF
AU  - Lazarević-Pašti, Tamara
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9318
AB  - Some organophosphorous pesticides (OPs) containing phosphorthioate group were
oxidized in vitro by enzyme myeloperoxidase (MPO) in the presence of hydrogen
peroxide. The products were identified as oxon derivatives (phosphates), where the
sulfur atom from thioate group is substituted by an oxygen atom. The oxidation
efficiency was determined using acethylcholinesterase (AChE) bioassay and discused
in the terms of MPO concentration, OPs concentration and incubation time.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
T1  - Oxidation of some organophosphate pesticides with enzyme myeloperoxidase
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9318
ER  - 

@conference{
author = "Lazarević-Pašti, Tamara and Momić, Tatjana and Vasić, Vesna M.",
year = "2010",
abstract = "Some organophosphorous pesticides (OPs) containing phosphorthioate group were
oxidized in vitro by enzyme myeloperoxidase (MPO) in the presence of hydrogen
peroxide. The products were identified as oxon derivatives (phosphates), where the
sulfur atom from thioate group is substituted by an oxygen atom. The oxidation
efficiency was determined using acethylcholinesterase (AChE) bioassay and discused
in the terms of MPO concentration, OPs concentration and incubation time.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry",
title = "Oxidation of some organophosphate pesticides with enzyme myeloperoxidase",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9318"
}

Lazarević-Pašti, T., Momić, T.,& Vasić, V. M.. (2010). Oxidation of some organophosphate pesticides with enzyme myeloperoxidase. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia..
https://hdl.handle.net/21.15107/rcub_vinar_9318

Lazarević-Pašti T, Momić T, Vasić VM. Oxidation of some organophosphate pesticides with enzyme myeloperoxidase. in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry. 2010;.
https://hdl.handle.net/21.15107/rcub_vinar_9318 .

Lazarević-Pašti, Tamara, Momić, Tatjana, Vasić, Vesna M., "Oxidation of some organophosphate pesticides with enzyme myeloperoxidase" in Physical chemistry 2010 : 10th international conference on fundamental and applied aspects of physical chemistry (2010),
https://hdl.handle.net/21.15107/rcub_vinar_9318 .

TY  - JOUR
AU  - Petković, Marijana
AU  - Petrović, Biljana
AU  - Savić, Jasmina
AU  - Bugarčić, Živadin D.
AU  - Dimitrić-Marković, Jasmina
AU  - Momić, Tatjana
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3909
AB  - Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a suitable method for the analysis of inorganic and organic compounds and biomolecules This makes. MALDI-TOF MS convenient for monitoring the interaction of metallo-drugs with biomolecules. Results presented in this manuscript demonstrate that flavonoids such as apigenin, kaempferol and luteolin are suitable for MALDI-TOF MS analysis of Pt(II), Pd(II), Pt(IV) and Ru(III) complexes, giving different signal-to-noise ratios of the analyte peak. The MALDI-TOF mass spectra of inorganic complexes acquired with these flavonoid matrices are easy to interpret and have some advantages over the application of other commonly used matrices: a low number of matrix peaks are detectable and the coordinative metal-ligand bond is, in most cases, preserved. On the other hand, flavonoids do not act as typical matrices, as their excess is not required for the acquisition of MALDI-TOF mass spectra of inorganic complexes. (C) 2009 Elsevier B.V. All rights reserved.
T2  - International Journal of Mass Spectrometry
T1  - Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes
VL  - 290
IS  - 1
SP  - 39
EP  - 46
DO  - 10.1016/j.ijms.2009.12.001
ER  - 

@article{
author = "Petković, Marijana and Petrović, Biljana and Savić, Jasmina and Bugarčić, Živadin D. and Dimitrić-Marković, Jasmina and Momić, Tatjana and Vasić, Vesna M.",
year = "2010",
abstract = "Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS) is a suitable method for the analysis of inorganic and organic compounds and biomolecules This makes. MALDI-TOF MS convenient for monitoring the interaction of metallo-drugs with biomolecules. Results presented in this manuscript demonstrate that flavonoids such as apigenin, kaempferol and luteolin are suitable for MALDI-TOF MS analysis of Pt(II), Pd(II), Pt(IV) and Ru(III) complexes, giving different signal-to-noise ratios of the analyte peak. The MALDI-TOF mass spectra of inorganic complexes acquired with these flavonoid matrices are easy to interpret and have some advantages over the application of other commonly used matrices: a low number of matrix peaks are detectable and the coordinative metal-ligand bond is, in most cases, preserved. On the other hand, flavonoids do not act as typical matrices, as their excess is not required for the acquisition of MALDI-TOF mass spectra of inorganic complexes. (C) 2009 Elsevier B.V. All rights reserved.",
journal = "International Journal of Mass Spectrometry",
title = "Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes",
volume = "290",
number = "1",
pages = "39-46",
doi = "10.1016/j.ijms.2009.12.001"
}

Petković, M., Petrović, B., Savić, J., Bugarčić, Ž. D., Dimitrić-Marković, J., Momić, T.,& Vasić, V. M.. (2010). Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes. in International Journal of Mass Spectrometry, 290(1), 39-46.
https://doi.org/10.1016/j.ijms.2009.12.001

Petković M, Petrović B, Savić J, Bugarčić ŽD, Dimitrić-Marković J, Momić T, Vasić VM. Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes. in International Journal of Mass Spectrometry. 2010;290(1):39-46.
doi:10.1016/j.ijms.2009.12.001 .

Petković, Marijana, Petrović, Biljana, Savić, Jasmina, Bugarčić, Živadin D., Dimitrić-Marković, Jasmina, Momić, Tatjana, Vasić, Vesna M., "Flavonoids as matrices for MALDI-TOF mass spectrometric analysis of transition metal complexes" in International Journal of Mass Spectrometry, 290, no. 1 (2010):39-46,
https://doi.org/10.1016/j.ijms.2009.12.001 . .

TY  - JOUR
AU  - Lazarević-Pašti, Tamara
AU  - Momić, Tatjana
AU  - Onjia, Antonije E.
AU  - Vujisić, Ljubodrag
AU  - Vasić, Vesna M.
PY  - 2010
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/4092
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.
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 and Momić, Tatjana and Onjia, Antonije E. and Vujisić, Ljubodrag and Vasić, Vesna M.",
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.",
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., Momić, T., Onjia, A. E., Vujisić, L.,& Vasić, V. M.. (2010). Myeloperoxidase-mediated oxidation of organophosphorus pesticides as a pre-step in their determination by AChE based bioanalytical methods. in Microchimica Acta, 170(3-4), 289-297.
https://doi.org/10.1007/s00604-010-0324-2

Lazarević-Pašti T, Momić T, Onjia AE, Vujisić L, Vasić VM. 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, Momić, Tatjana, Onjia, Antonije E., Vujisić, Ljubodrag, Vasić, Vesna M., "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 . .

TY  - JOUR
AU  - Čolović, Mirjana B.
AU  - Krstić, Danijela Z.
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Savić, Jasmina
AU  - Vujačić, Ana V.
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/6815
AB  - The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity induced by some specific and non specific inhibitors. For this purpose, the effects of some ouabain like compounds (digoxin, gitoxin), noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+), and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase from rat synaptic plasma membranes (SPM), porcine cerebral cortex and human erythrocytes were discussed.
T2  - Russian Journal of Physical Chemistry A
T1  - Na+/K+-ATPase: Activity and inhibition
VL  - 83
IS  - 9
SP  - 1602
EP  - 1608
DO  - 10.1134/S0036024409090337
ER  - 

@article{
author = "Čolović, Mirjana B. and Krstić, Danijela Z. and Krinulović, Katarina and Momić, Tatjana and Savić, Jasmina and Vujačić, Ana V. and Vasić, Vesna M.",
year = "2009",
abstract = "The aim of the study was to give an overview of the mechanism of inhibition of Na+/K+-ATPase activity induced by some specific and non specific inhibitors. For this purpose, the effects of some ouabain like compounds (digoxin, gitoxin), noble metals complexes ([PtCl2DMSO2], [AuCl4](-), [PdCl4](2-), [PdCl(dien)](+), [PdCl(Me(4)dien)](+)), transition metal ions (Cu2+, Zn2+, Fe2+, Co2+), and heavy metal ions (Hg2+, Pb2+, Cd2+) on the activity of Na+/K+-ATPase from rat synaptic plasma membranes (SPM), porcine cerebral cortex and human erythrocytes were discussed.",
journal = "Russian Journal of Physical Chemistry A",
title = "Na+/K+-ATPase: Activity and inhibition",
volume = "83",
number = "9",
pages = "1602-1608",
doi = "10.1134/S0036024409090337"
}

Čolović, M. B., Krstić, D. Z., Krinulović, K., Momić, T., Savić, J., Vujačić, A. V.,& Vasić, V. M.. (2009). Na+/K+-ATPase: Activity and inhibition. in Russian Journal of Physical Chemistry A, 83(9), 1602-1608.
https://doi.org/10.1134/S0036024409090337

Čolović MB, Krstić DZ, Krinulović K, Momić T, Savić J, Vujačić AV, Vasić VM. Na+/K+-ATPase: Activity and inhibition. in Russian Journal of Physical Chemistry A. 2009;83(9):1602-1608.
doi:10.1134/S0036024409090337 .

Čolović, Mirjana B., Krstić, Danijela Z., Krinulović, Katarina, Momić, Tatjana, Savić, Jasmina, Vujačić, Ana V., Vasić, Vesna M., "Na+/K+-ATPase: Activity and inhibition" in Russian Journal of Physical Chemistry A, 83, no. 9 (2009):1602-1608,
https://doi.org/10.1134/S0036024409090337 . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Momić, Tatjana
AU  - Petković, Marijana
AU  - Krstić, Danijela Z.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3626
T2  - Sensors
T1  - Correction: Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds (vol 8, pg 8321, 2008)
VL  - 9
IS  - 1
SP  - 377
EP  - 377
DO  - 10.3390/s90100377
ER  - 

@article{
author = "Vasić, Vesna M. and Momić, Tatjana and Petković, Marijana and Krstić, Danijela Z.",
year = "2009",
journal = "Sensors",
title = "Correction: Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds (vol 8, pg 8321, 2008)",
volume = "9",
number = "1",
pages = "377-377",
doi = "10.3390/s90100377"
}

Vasić, V. M., Momić, T., Petković, M.,& Krstić, D. Z.. (2009). Correction: Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds (vol 8, pg 8321, 2008). in Sensors, 9(1), 377-377.
https://doi.org/10.3390/s90100377

Vasić VM, Momić T, Petković M, Krstić DZ. Correction: Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds (vol 8, pg 8321, 2008). in Sensors. 2009;9(1):377-377.
doi:10.3390/s90100377 .

Vasić, Vesna M., Momić, Tatjana, Petković, Marijana, Krstić, Danijela Z., "Correction: Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds (vol 8, pg 8321, 2008)" in Sensors, 9, no. 1 (2009):377-377,
https://doi.org/10.3390/s90100377 . .

TY  - CONF
AU  - Savić, Jasmina
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Čolović, Mirjana B.
AU  - Vujačić, Ana V.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9354
AB  - An ion-pair ultra performance liquid chromatography (IP-UPLC) method was developed to obtain a sensitive and efficient means for quantification of ADP in order to follow the decrease of Na+ /K+  ATPase activity after its exposure to different inhibitors. The concentrations of ADP obtained after hydrolysis of ATP in the presence of enzyme depends on enzyme activity. Simultaneously with the chromatographic determination of ADP, the spectrophotometric determination of phosphates liberated after the hydrolysis of ATP was done.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity
VL  - 1
SP  - 36
EP  - 38
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9354
ER  - 

@conference{
author = "Savić, Jasmina and Krinulović, Katarina and Momić, Tatjana and Čolović, Mirjana B. and Vujačić, Ana V.",
year = "2008",
abstract = "An ion-pair ultra performance liquid chromatography (IP-UPLC) method was developed to obtain a sensitive and efficient means for quantification of ADP in order to follow the decrease of Na+ /K+  ATPase activity after its exposure to different inhibitors. The concentrations of ADP obtained after hydrolysis of ATP in the presence of enzyme depends on enzyme activity. Simultaneously with the chromatographic determination of ADP, the spectrophotometric determination of phosphates liberated after the hydrolysis of ATP was done.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity",
volume = "1",
pages = "36-38",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9354"
}

Savić, J., Krinulović, K., Momić, T., Čolović, M. B.,& Vujačić, A. V.. (2008). Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 36-38.
https://hdl.handle.net/21.15107/rcub_vinar_9354

Savić J, Krinulović K, Momić T, Čolović MB, Vujačić AV. Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:36-38.
https://hdl.handle.net/21.15107/rcub_vinar_9354 .

Savić, Jasmina, Krinulović, Katarina, Momić, Tatjana, Čolović, Mirjana B., Vujačić, Ana V., "Application of ultra performance liquid chromatography (uplc) for determination of Na+ /K+ atpase activity" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):36-38,
https://hdl.handle.net/21.15107/rcub_vinar_9354 .

TY  - CONF
AU  - Savić, Jasmina
AU  - Momić, Tatjana
AU  - Milenković, Aleksandra S.
AU  - Vujačić, Ana V.
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9360
AB  - The equilibrium and kinetics of the reaction between tetrachloroaurate(III) ion (AuCl4 - ) and quercetin in 0.1 M HClO4 were studied spectrophotometrically. The fast and the slow reaction steps were distinguished in the reaction mechanism, depending on the ratio of AuCl4 -  and quercetin concentration. The stoichiometry of reaction, determined by molar ratio and Jobb’s methods, was 1:1. The kinetics of complex formation was followed under the pseudo-first order conditions by measuring the absorbance at 294 nm vs. time as the function of quercetin concentration in 5 – 15 fold excess.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
T1  - Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin
VL  - 1
SP  - 172
EP  - 174
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9360
ER  - 

@conference{
author = "Savić, Jasmina and Momić, Tatjana and Milenković, Aleksandra S. and Vujačić, Ana V. and Vasić, Vesna M.",
year = "2008",
abstract = "The equilibrium and kinetics of the reaction between tetrachloroaurate(III) ion (AuCl4 - ) and quercetin in 0.1 M HClO4 were studied spectrophotometrically. The fast and the slow reaction steps were distinguished in the reaction mechanism, depending on the ratio of AuCl4 -  and quercetin concentration. The stoichiometry of reaction, determined by molar ratio and Jobb’s methods, was 1:1. The kinetics of complex formation was followed under the pseudo-first order conditions by measuring the absorbance at 294 nm vs. time as the function of quercetin concentration in 5 – 15 fold excess.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry",
title = "Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin",
volume = "1",
pages = "172-174",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9360"
}

Savić, J., Momić, T., Milenković, A. S., Vujačić, A. V.,& Vasić, V. M.. (2008). Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry
Society of Physical Chemists of Serbia., 1, 172-174.
https://hdl.handle.net/21.15107/rcub_vinar_9360

Savić J, Momić T, Milenković AS, Vujačić AV, Vasić VM. Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin. in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry. 2008;1:172-174.
https://hdl.handle.net/21.15107/rcub_vinar_9360 .

Savić, Jasmina, Momić, Tatjana, Milenković, Aleksandra S., Vujačić, Ana V., Vasić, Vesna M., "Spectrophotometric and uplc study of reaction between [AuCl4] - and quercetin" in Physical chemistry 2008 : 9th international conference on fundamental and applied aspects of physical chemistry, 1 (2008):172-174,
https://hdl.handle.net/21.15107/rcub_vinar_9360 .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Momić, Tatjana
AU  - Petković, Marijana
AU  - Krstić, Danijela Z.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3598
AB  - This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na+,K+-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na+,K+-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na+,K+-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research.
T2  - Sensors
T1  - Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds
VL  - 8
IS  - 12
SP  - 8321
EP  - 8360
DO  - 10.3390/s8128321
ER  - 

@article{
author = "Vasić, Vesna M. and Momić, Tatjana and Petković, Marijana and Krstić, Danijela Z.",
year = "2008",
abstract = "This paper gives an overview of the literature data concerning specific and non specific inhibitors of Na+,K+-ATPase receptor. The immobilization approaches developed to improve the rather low time and temperature stability of Na+,K+-ATPase, as well to preserve the enzyme properties were overviewed. The functional immobilization of Na+,K+-ATPase receptor as the target, with preservation of the full functional protein activity and access of various substances to an optimum number of binding sites under controlled conditions in the combination with high sensitive technology for the detection of enzyme activity is the basis for application of this enzyme in medical, pharmaceutical and environmental research.",
journal = "Sensors",
title = "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds",
volume = "8",
number = "12",
pages = "8321-8360",
doi = "10.3390/s8128321"
}

Vasić, V. M., Momić, T., Petković, M.,& Krstić, D. Z.. (2008). Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors, 8(12), 8321-8360.
https://doi.org/10.3390/s8128321

Vasić VM, Momić T, Petković M, Krstić DZ. Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds. in Sensors. 2008;8(12):8321-8360.
doi:10.3390/s8128321 .

Vasić, Vesna M., Momić, Tatjana, Petković, Marijana, Krstić, Danijela Z., "Na+,K+-ATPase as the Target Enzyme for Organic and Inorganic Compounds" in Sensors, 8, no. 12 (2008):8321-8360,
https://doi.org/10.3390/s8128321 . .

TY  - JOUR
AU  - Vasić, Vesna M.
AU  - Krinulović, Katarina
AU  - Momić, Tatjana
AU  - Čolović, Mirjana B.
AU  - Vujačić, Ana V.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3550
AB  - The influence of some organic compounds (pyridine, urea, chlorpyrifos, permethrin) and metal ions (Pb2+, Cd2-, Hg2+, Cu2+, Fe2+ and Zn2+) on Na+/K+-ATPase and Mg2+-ATpase activity isolated from rat brain synaptic plasma membranes (SPM) was investigated in order to develop a simple semi-quantitative and qualitative test method for selective detection of these analyites in aqueous solutions. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-p liberated by enzyme-catalysed hydrolysis of adenosinetriphosphate (ATP), by exposure to analytes was dose-dependent on the analyte concentration. Heavy metals (Pb, Cd, Hg, Cu, Fe and Zn), toxic organic compounds (pyridine, urea) and some pesticides (ehlorpyrifos, permethrin) showed diverse effects, inducing the inhibition or stimulation of the enzyme activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.
T2  - Journal of Environmental Protection and Ecology
T1  - Effects of Some Organic and Inorganic Compounds on Atpase Activity
VL  - 9
IS  - 3
SP  - 583
EP  - 591
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3550
ER  - 

@article{
author = "Vasić, Vesna M. and Krinulović, Katarina and Momić, Tatjana and Čolović, Mirjana B. and Vujačić, Ana V.",
year = "2008",
abstract = "The influence of some organic compounds (pyridine, urea, chlorpyrifos, permethrin) and metal ions (Pb2+, Cd2-, Hg2+, Cu2+, Fe2+ and Zn2+) on Na+/K+-ATPase and Mg2+-ATpase activity isolated from rat brain synaptic plasma membranes (SPM) was investigated in order to develop a simple semi-quantitative and qualitative test method for selective detection of these analyites in aqueous solutions. The method is based on the spectrophotometric determination of inorganic ortho-phosphate (P-i) that serves as a measure of the enzymatic activity in the presence of various analytes. The concentration of P-p liberated by enzyme-catalysed hydrolysis of adenosinetriphosphate (ATP), by exposure to analytes was dose-dependent on the analyte concentration. Heavy metals (Pb, Cd, Hg, Cu, Fe and Zn), toxic organic compounds (pyridine, urea) and some pesticides (ehlorpyrifos, permethrin) showed diverse effects, inducing the inhibition or stimulation of the enzyme activity. Development of simple test method for simultaneous detection of the investigated analytes based on the variation of medium assay composition was discussed.",
journal = "Journal of Environmental Protection and Ecology",
title = "Effects of Some Organic and Inorganic Compounds on Atpase Activity",
volume = "9",
number = "3",
pages = "583-591",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3550"
}

Vasić, V. M., Krinulović, K., Momić, T., Čolović, M. B.,& Vujačić, A. V.. (2008). Effects of Some Organic and Inorganic Compounds on Atpase Activity. in Journal of Environmental Protection and Ecology, 9(3), 583-591.
https://hdl.handle.net/21.15107/rcub_vinar_3550

Vasić VM, Krinulović K, Momić T, Čolović MB, Vujačić AV. Effects of Some Organic and Inorganic Compounds on Atpase Activity. in Journal of Environmental Protection and Ecology. 2008;9(3):583-591.
https://hdl.handle.net/21.15107/rcub_vinar_3550 .

Vasić, Vesna M., Krinulović, Katarina, Momić, Tatjana, Čolović, Mirjana B., Vujačić, Ana V., "Effects of Some Organic and Inorganic Compounds on Atpase Activity" in Journal of Environmental Protection and Ecology, 9, no. 3 (2008):583-591,
https://hdl.handle.net/21.15107/rcub_vinar_3550 .

TY  - JOUR
AU  - Momić, Tatjana
AU  - Vujčić, Zoran
AU  - Vasić, Vesna M.
PY  - 2008
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3464
AB  - The inhibition of myeloperoxidase (MPO), isolated from human neutrophils, by quercetin was investigated by following peroxidase activity of the enzyme using o-dianisidine as the substrate. The inhibition parameters (IC(50)) were obtained by graphical analysis of the inhibition curves. A reaction mechanism, which involved the enzyme inhibition by quercetin and H(2)O(2) in excess, was proposed. The rate and equilibrium constants for the proposed reaction path were calculated from experimental data. Kinetic analysis in noninhibiting H(2)O(2) concentration range in the absence and the presence of quercetin revealed that the reaction mechanism underwent Michaelis-Menten kinetics. K(m)(app,H2O2) and V(max)(app) values indicated that quercetin was a mixed inhibitor of MPO activity. The initial reaction rates were recalculated using the obtained results. Calculated curves fitted the experimental results within the range of experimental error. (C) 2008 Wiley Periodicals, Inc.
T2  - International Journal of Chemical Kinetics
T1  - Kinetics of inhibition of peroxidase activity of myeloperoxidase by quercetin
VL  - 40
IS  - 7
SP  - 384
EP  - 394
DO  - 10.1002/kin.20319
ER  - 

@article{
author = "Momić, Tatjana and Vujčić, Zoran and Vasić, Vesna M.",
year = "2008",
abstract = "The inhibition of myeloperoxidase (MPO), isolated from human neutrophils, by quercetin was investigated by following peroxidase activity of the enzyme using o-dianisidine as the substrate. The inhibition parameters (IC(50)) were obtained by graphical analysis of the inhibition curves. A reaction mechanism, which involved the enzyme inhibition by quercetin and H(2)O(2) in excess, was proposed. The rate and equilibrium constants for the proposed reaction path were calculated from experimental data. Kinetic analysis in noninhibiting H(2)O(2) concentration range in the absence and the presence of quercetin revealed that the reaction mechanism underwent Michaelis-Menten kinetics. K(m)(app,H2O2) and V(max)(app) values indicated that quercetin was a mixed inhibitor of MPO activity. The initial reaction rates were recalculated using the obtained results. Calculated curves fitted the experimental results within the range of experimental error. (C) 2008 Wiley Periodicals, Inc.",
journal = "International Journal of Chemical Kinetics",
title = "Kinetics of inhibition of peroxidase activity of myeloperoxidase by quercetin",
volume = "40",
number = "7",
pages = "384-394",
doi = "10.1002/kin.20319"
}

Momić, T., Vujčić, Z.,& Vasić, V. M.. (2008). Kinetics of inhibition of peroxidase activity of myeloperoxidase by quercetin. in International Journal of Chemical Kinetics, 40(7), 384-394.
https://doi.org/10.1002/kin.20319

Momić T, Vujčić Z, Vasić VM. Kinetics of inhibition of peroxidase activity of myeloperoxidase by quercetin. in International Journal of Chemical Kinetics. 2008;40(7):384-394.
doi:10.1002/kin.20319 .

Momić, Tatjana, Vujčić, Zoran, Vasić, Vesna M., "Kinetics of inhibition of peroxidase activity of myeloperoxidase by quercetin" in International Journal of Chemical Kinetics, 40, no. 7 (2008):384-394,
https://doi.org/10.1002/kin.20319 . .

TY  - JOUR
AU  - Momić, Tatjana
AU  - Savić, Jasmina
AU  - Černigoj, Urh
AU  - Trebše, Polonca
AU  - Vasić, Vesna M.
PY  - 2007
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3355
AB  - Studies of protolytic equilibria and investigations of stability of flavonoids at different acidities are necessary to better understand their antioxidant efficiencies and autoxidation characteristics. The protonation constant of carbonyl group and dissociation constants of OH groups of quercetin in aqueous solutions were determined spectrophotometrically. The distribution diagram of ionic species in aqueous solutions of various acidities was calculated. Study of the effects of UV irradiation on quercetin at pH 5.00, 7.50 and 10.00 indicated that UV irradiation accelerated quercetin autoxidation via the formation of the oxidation product. The stability of quercetin and oxidation product was investigated as a function of irradiation time by using spectrophotometric and HPLC techniques. The apparent pseudo-first-order rate constants for quercetin degradation and oxidation product formation were calculated and discussed.
T2  - Collection of Czechoslovak Chemical Communications
T1  - Protolytic equilibria and photodegradation of quercetin in aqueous solution
VL  - 72
IS  - 11
SP  - 1447
EP  - 1460
DO  - 10.1135/cccc20071447
ER  - 

@article{
author = "Momić, Tatjana and Savić, Jasmina and Černigoj, Urh and Trebše, Polonca and Vasić, Vesna M.",
year = "2007",
abstract = "Studies of protolytic equilibria and investigations of stability of flavonoids at different acidities are necessary to better understand their antioxidant efficiencies and autoxidation characteristics. The protonation constant of carbonyl group and dissociation constants of OH groups of quercetin in aqueous solutions were determined spectrophotometrically. The distribution diagram of ionic species in aqueous solutions of various acidities was calculated. Study of the effects of UV irradiation on quercetin at pH 5.00, 7.50 and 10.00 indicated that UV irradiation accelerated quercetin autoxidation via the formation of the oxidation product. The stability of quercetin and oxidation product was investigated as a function of irradiation time by using spectrophotometric and HPLC techniques. The apparent pseudo-first-order rate constants for quercetin degradation and oxidation product formation were calculated and discussed.",
journal = "Collection of Czechoslovak Chemical Communications",
title = "Protolytic equilibria and photodegradation of quercetin in aqueous solution",
volume = "72",
number = "11",
pages = "1447-1460",
doi = "10.1135/cccc20071447"
}

Momić, T., Savić, J., Černigoj, U., Trebše, P.,& Vasić, V. M.. (2007). Protolytic equilibria and photodegradation of quercetin in aqueous solution. in Collection of Czechoslovak Chemical Communications, 72(11), 1447-1460.
https://doi.org/10.1135/cccc20071447

Momić T, Savić J, Černigoj U, Trebše P, Vasić VM. Protolytic equilibria and photodegradation of quercetin in aqueous solution. in Collection of Czechoslovak Chemical Communications. 2007;72(11):1447-1460.
doi:10.1135/cccc20071447 .

Momić, Tatjana, Savić, Jasmina, Černigoj, Urh, Trebše, Polonca, Vasić, Vesna M., "Protolytic equilibria and photodegradation of quercetin in aqueous solution" in Collection of Czechoslovak Chemical Communications, 72, no. 11 (2007):1447-1460,
https://doi.org/10.1135/cccc20071447 . .

TY  - CONF
AU  - Momić, Tatjana
AU  - Vujčić, Zoran
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9425
AB  - Reaction mechanism of quercetin induced inhibition of myeloperoxidase isolated from human neutrophils was proposed by following peroxidase activity of the enzyme, using the o-dianisidine and H2O2 as substrates. The dependence of initial reaction rate vs. H2O2 concentration in the absence and presence of quercetin revealed the reaction mechanism that involved the enzyme inhibition by the excess of the substrate. The rate and equililbria constants for proposed reaction paths were determined
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
T1  - Inhibition of myeloperoxidase by quercetin
SP  - 359
EP  - 361
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9425
ER  - 

@conference{
author = "Momić, Tatjana and Vujčić, Zoran and Vasić, Vesna M.",
year = "2006",
abstract = "Reaction mechanism of quercetin induced inhibition of myeloperoxidase isolated from human neutrophils was proposed by following peroxidase activity of the enzyme, using the o-dianisidine and H2O2 as substrates. The dependence of initial reaction rate vs. H2O2 concentration in the absence and presence of quercetin revealed the reaction mechanism that involved the enzyme inhibition by the excess of the substrate. The rate and equililbria constants for proposed reaction paths were determined",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry",
title = "Inhibition of myeloperoxidase by quercetin",
pages = "359-361",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9425"
}

Momić, T., Vujčić, Z.,& Vasić, V. M.. (2006). Inhibition of myeloperoxidase by quercetin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 359-361.
https://hdl.handle.net/21.15107/rcub_vinar_9425

Momić T, Vujčić Z, Vasić VM. Inhibition of myeloperoxidase by quercetin. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry. 2006;:359-361.
https://hdl.handle.net/21.15107/rcub_vinar_9425 .

Momić, Tatjana, Vujčić, Zoran, Vasić, Vesna M., "Inhibition of myeloperoxidase by quercetin" in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry (2006):359-361,
https://hdl.handle.net/21.15107/rcub_vinar_9425 .

TY  - CONF
AU  - Momić, Tatjana
AU  - Savić, Jasmina
AU  - Miljević, Nada R.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/9424
AB  - The protonation constant of carbonyl group and dissociation constants of -OH groups of quercetin were determined from the changes in UV and IR spectra of aqueous solutions of various acidities. The distribution diagram of ionic species was calculated. Besides, the stability of quercetin was investigated as the function of pH and concentration. The analysis of kinetic curves indicated that a noncatalyzed conversion took place together with the autocatalyzed degradation of quercetin.
PB  - Society of Physical Chemists of Serbia
C3  - Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
T1  - Protolytic equilibria and stability of quercetin in aqueous solutions
SP  - 356
EP  - 358
UR  - https://hdl.handle.net/21.15107/rcub_vinar_9424
ER  - 

@conference{
author = "Momić, Tatjana and Savić, Jasmina and Miljević, Nada R.",
year = "2006",
abstract = "The protonation constant of carbonyl group and dissociation constants of -OH groups of quercetin were determined from the changes in UV and IR spectra of aqueous solutions of various acidities. The distribution diagram of ionic species was calculated. Besides, the stability of quercetin was investigated as the function of pH and concentration. The analysis of kinetic curves indicated that a noncatalyzed conversion took place together with the autocatalyzed degradation of quercetin.",
publisher = "Society of Physical Chemists of Serbia",
journal = "Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry",
title = "Protolytic equilibria and stability of quercetin in aqueous solutions",
pages = "356-358",
url = "https://hdl.handle.net/21.15107/rcub_vinar_9424"
}

Momić, T., Savić, J.,& Miljević, N. R.. (2006). Protolytic equilibria and stability of quercetin in aqueous solutions. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry
Society of Physical Chemists of Serbia., 356-358.
https://hdl.handle.net/21.15107/rcub_vinar_9424

Momić T, Savić J, Miljević NR. Protolytic equilibria and stability of quercetin in aqueous solutions. in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry. 2006;:356-358.
https://hdl.handle.net/21.15107/rcub_vinar_9424 .

Momić, Tatjana, Savić, Jasmina, Miljević, Nada R., "Protolytic equilibria and stability of quercetin in aqueous solutions" in Physical chemistry 2006: 8th international conference on fundemental and applied aspract of physical chemistry (2006):356-358,
https://hdl.handle.net/21.15107/rcub_vinar_9424 .

TY  - JOUR
AU  - Horvat, Anica
AU  - Momić, Tatjana
AU  - Banjac, Ana
AU  - Petrović S.
AU  - Nikezić, Gordana S.
AU  - Demajo, Miroslav
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3040
AB  - The effect of drugs from the class of cardiac (methyldigoxin, verapamil, propranolol), antiepileptic ( carbamazepine), sedative (diazepam) and antihistaminic (promethazine) drugs on Na,K-ATPase activity of plasma membranes was studied in rat brain synaptosomes. Methyldigoxin in a concentration of 0.1 mmol/l inhibits enzyme activity by 80%. Verapamil, propranolol and promethazine in concentrations of 20, 20 and 2 mmol/l respectively, entirely inhibit the ATPase activity. Carbamazepine and diazepam in concentrations of 0.02-60 mmol/l have no effect on the activity of this enzyme. According to the drug concentrations that inhibit 50% of enzyme activity (IC50), the potency can be listed in the following order: methyldigoxin GT GT promethazine GT verapamil GT = propranolol. From the inhibition of commercially available purified Na, K-ATPase isolated from porcine cerebral cortex in the presence of chosen drugs, as well as from kinetic studies on synaptosomal plasma membranes, it may be concluded that the drugs inhibit enzyme activity, partly by acting directly on the enzyme proteins. Propranolol, verapamil and promethazine inhibitions acted in an uncompetitive manner. The results suggest that these three drugs may contribute to neurological dysfunctions and indicate the necessity to take into consideration the side effects of the investigated drugs during the treatment of various pathological conditions.
T2  - Physiological Research
T1  - Selective inhibition of brain Na,K-ATPase by drugs
VL  - 55
IS  - 3
SP  - 325
EP  - 338
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3040
ER  - 

@article{
author = "Horvat, Anica and Momić, Tatjana and Banjac, Ana and Petrović S. and Nikezić, Gordana S. and Demajo, Miroslav",
year = "2006",
abstract = "The effect of drugs from the class of cardiac (methyldigoxin, verapamil, propranolol), antiepileptic ( carbamazepine), sedative (diazepam) and antihistaminic (promethazine) drugs on Na,K-ATPase activity of plasma membranes was studied in rat brain synaptosomes. Methyldigoxin in a concentration of 0.1 mmol/l inhibits enzyme activity by 80%. Verapamil, propranolol and promethazine in concentrations of 20, 20 and 2 mmol/l respectively, entirely inhibit the ATPase activity. Carbamazepine and diazepam in concentrations of 0.02-60 mmol/l have no effect on the activity of this enzyme. According to the drug concentrations that inhibit 50% of enzyme activity (IC50), the potency can be listed in the following order: methyldigoxin GT GT promethazine GT verapamil GT = propranolol. From the inhibition of commercially available purified Na, K-ATPase isolated from porcine cerebral cortex in the presence of chosen drugs, as well as from kinetic studies on synaptosomal plasma membranes, it may be concluded that the drugs inhibit enzyme activity, partly by acting directly on the enzyme proteins. Propranolol, verapamil and promethazine inhibitions acted in an uncompetitive manner. The results suggest that these three drugs may contribute to neurological dysfunctions and indicate the necessity to take into consideration the side effects of the investigated drugs during the treatment of various pathological conditions.",
journal = "Physiological Research",
title = "Selective inhibition of brain Na,K-ATPase by drugs",
volume = "55",
number = "3",
pages = "325-338",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3040"
}

Horvat, A., Momić, T., Banjac, A., Petrović S., Nikezić, G. S.,& Demajo, M.. (2006). Selective inhibition of brain Na,K-ATPase by drugs. in Physiological Research, 55(3), 325-338.
https://hdl.handle.net/21.15107/rcub_vinar_3040

Horvat A, Momić T, Banjac A, Petrović S., Nikezić GS, Demajo M. Selective inhibition of brain Na,K-ATPase by drugs. in Physiological Research. 2006;55(3):325-338.
https://hdl.handle.net/21.15107/rcub_vinar_3040 .

Horvat, Anica, Momić, Tatjana, Banjac, Ana, Petrović S., Nikezić, Gordana S., Demajo, Miroslav, "Selective inhibition of brain Na,K-ATPase by drugs" in Physiological Research, 55, no. 3 (2006):325-338,
https://hdl.handle.net/21.15107/rcub_vinar_3040 .