TY  - JOUR
AU  - Filipović, Nenad
AU  - Bjelogrlić, Snežana
AU  - Marinković, Aleksandar
AU  - Verbić, Tatjana Z.
AU  - Cvijetić, Ilija N.
AU  - Sencanski, Milan
AU  - Rodić, Marko
AU  - Vujcić, Miroslava
AU  - Sladić, Dušan M.
AU  - Striković, Zlatko
AU  - Todorović, Tamara R.
AU  - Muller, Christian D.
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3749
AB  - A new Zn(II)-based potential chemotherapeutic agent was synthesized from the ligand 2-quinolinecarboxaldehyde selenosemicarbazone (Hqasesc). Single crystal X-ray diffraction analysis showed that the Zn(II) complex consists of a cation [Zn(Hqasesc)(2)](2+), two perchlorate anions and one ethanol solvent molecule. The interaction of calf thymus (CT) DNA and human serum albumin (HSA) with the Zn(II) complex was explored using absorption and emission spectral methods, and also has been supported by molecular docking studies. The complex has more affinity to minor DNA groove than major, with no significant intercalation. The HSA interaction studies of the complex revealed the quenching of the intrinsic fluorescence of the HSA through a static quenching mechanism. The antitumor activity of the ligand and the complex against pancreatic adenocarcinoma cell line (AsPC-1) and acute monocytic leukemia (THP-1) cells was evaluated. Both compounds are strong concentration-dependent apoptosis inducers in THP-1 cells. While Hqasesc in AsPC-1 cells induces apoptosis only at the highest concentration, treatment with the Zn complex shows a concentration-dependent apoptotic response, where the treated cells are arrested in the G1-to-S phase accompanied with extensive activation of caspase-8 and -9. These results indicate that the ligand and Zn(II) complex display cell phenotype specific activity.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction
EP  - 95211
IS  - 115
SP  - 95191
VL  - 5
DO  - 10.1039/c5ra19849f
ER  - 

@article{
author = "Filipović, Nenad and Bjelogrlić, Snežana and Marinković, Aleksandar and Verbić, Tatjana Z. and Cvijetić, Ilija N. and Sencanski, Milan and Rodić, Marko and Vujcić, Miroslava and Sladić, Dušan M. and Striković, Zlatko and Todorović, Tamara R. and Muller, Christian D.",
year = "2015",
abstract = "A new Zn(II)-based potential chemotherapeutic agent was synthesized from the ligand 2-quinolinecarboxaldehyde selenosemicarbazone (Hqasesc). Single crystal X-ray diffraction analysis showed that the Zn(II) complex consists of a cation [Zn(Hqasesc)(2)](2+), two perchlorate anions and one ethanol solvent molecule. The interaction of calf thymus (CT) DNA and human serum albumin (HSA) with the Zn(II) complex was explored using absorption and emission spectral methods, and also has been supported by molecular docking studies. The complex has more affinity to minor DNA groove than major, with no significant intercalation. The HSA interaction studies of the complex revealed the quenching of the intrinsic fluorescence of the HSA through a static quenching mechanism. The antitumor activity of the ligand and the complex against pancreatic adenocarcinoma cell line (AsPC-1) and acute monocytic leukemia (THP-1) cells was evaluated. Both compounds are strong concentration-dependent apoptosis inducers in THP-1 cells. While Hqasesc in AsPC-1 cells induces apoptosis only at the highest concentration, treatment with the Zn complex shows a concentration-dependent apoptotic response, where the treated cells are arrested in the G1-to-S phase accompanied with extensive activation of caspase-8 and -9. These results indicate that the ligand and Zn(II) complex display cell phenotype specific activity.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction",
pages = "95211-95191",
number = "115",
volume = "5",
doi = "10.1039/c5ra19849f"
}

Filipović, N., Bjelogrlić, S., Marinković, A., Verbić, T. Z., Cvijetić, I. N., Sencanski, M., Rodić, M., Vujcić, M., Sladić, D. M., Striković, Z., Todorović, T. R.,& Muller, C. D.. (2015). Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction. in RSC Advances
Royal Soc Chemistry, Cambridge., 5(115), 95191-95211.
https://doi.org/10.1039/c5ra19849f

Filipović N, Bjelogrlić S, Marinković A, Verbić TZ, Cvijetić IN, Sencanski M, Rodić M, Vujcić M, Sladić DM, Striković Z, Todorović TR, Muller CD. Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction. in RSC Advances. 2015;5(115):95191-95211.
doi:10.1039/c5ra19849f .

Filipović, Nenad, Bjelogrlić, Snežana, Marinković, Aleksandar, Verbić, Tatjana Z., Cvijetić, Ilija N., Sencanski, Milan, Rodić, Marko, Vujcić, Miroslava, Sladić, Dušan M., Striković, Zlatko, Todorović, Tamara R., Muller, Christian D., "Zn(II) complex with 2-quinolinecarboxaldehyde selenosemicarbazone: synthesis, structure, interaction studies with DNA/HSA, molecular docking and caspase-8 and-9 independent apoptose induction" in RSC Advances, 5, no. 115 (2015):95191-95211,
https://doi.org/10.1039/c5ra19849f . .

TY  - JOUR
AU  - Tamaš, Nenad
AU  - Dojnov, Biljana
AU  - Margetić, Aleksandra
AU  - Vujcić, Miroslava
AU  - Špirović, Bojana
AU  - Miletić, Novica
AU  - Stević, Milan
AU  - Vujcić, Zoran
PY  - 2015
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/3785
AB  - Introduction. Aphis pomi (De Geer) has developed resistance to organophosphate and carbamate insecticides, as a result of long-term application of these insecticides in conventional apple orchards. For many years, the only mechanism of resistance identified in aphids was overproduction of insecticide-detoxifying esterases. Materials and methods. Insecticide resistance of A. pomi, collected from two conventional apple orchards (localities of Radmilovac-RA and Bela Crkva-BC) and one organic apple orchard (locality of Surcin-SU), was tested by bioassays and biochemical assays. Results and discussion. Compared with LC50 values for the susceptible population (organic orchard), both populations from the conventional orchards were highly resistant to pirimicarb (234.5 and 52.9 times) and moderately resistant to dimethoate (10.7 and 9.0 times). Increased esterase activity was determined in these two resistant aphid populations. Each of them also produced one esterase isoform more than the susceptible population, when 1-naphthyl acetate was used as a substrate for zymographic detection; when 2-naphthyl acetate was used as a substrate, only one resistant population produced two new esterase isoforms. In one of the resistant populations acetylcholinesterase (AChE) was significantly less inhibited by pirimicarb than in the other resistant population and the susceptible population, which indicates that this population developed another resistance mechanism-Modification of AChE (MACE). Conclusion. Detoxification of insecticides by the metabolic resistance mechanism of esterase enzymes and mechanism of modification of AChE was proven in one aphid population (RA). The other population (BC) has developed only metabolic resistance (enhanced metabolism by esterases), without modification of the insecticide target site (AChE). Development of insecticide resistance was caused by long-term application of acetylcholinesterase inhibitors (organophosphates and carbamates) in these conventional orchards.
PB  - Edp Sciences S A, Les Ulis Cedex A
T2  - Fruits
T1  - Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)
EP  - 142
IS  - 3
SP  - 135
VL  - 70
DO  - 10.1051/fruits/2015005
ER  - 

@article{
author = "Tamaš, Nenad and Dojnov, Biljana and Margetić, Aleksandra and Vujcić, Miroslava and Špirović, Bojana and Miletić, Novica and Stević, Milan and Vujcić, Zoran",
year = "2015",
abstract = "Introduction. Aphis pomi (De Geer) has developed resistance to organophosphate and carbamate insecticides, as a result of long-term application of these insecticides in conventional apple orchards. For many years, the only mechanism of resistance identified in aphids was overproduction of insecticide-detoxifying esterases. Materials and methods. Insecticide resistance of A. pomi, collected from two conventional apple orchards (localities of Radmilovac-RA and Bela Crkva-BC) and one organic apple orchard (locality of Surcin-SU), was tested by bioassays and biochemical assays. Results and discussion. Compared with LC50 values for the susceptible population (organic orchard), both populations from the conventional orchards were highly resistant to pirimicarb (234.5 and 52.9 times) and moderately resistant to dimethoate (10.7 and 9.0 times). Increased esterase activity was determined in these two resistant aphid populations. Each of them also produced one esterase isoform more than the susceptible population, when 1-naphthyl acetate was used as a substrate for zymographic detection; when 2-naphthyl acetate was used as a substrate, only one resistant population produced two new esterase isoforms. In one of the resistant populations acetylcholinesterase (AChE) was significantly less inhibited by pirimicarb than in the other resistant population and the susceptible population, which indicates that this population developed another resistance mechanism-Modification of AChE (MACE). Conclusion. Detoxification of insecticides by the metabolic resistance mechanism of esterase enzymes and mechanism of modification of AChE was proven in one aphid population (RA). The other population (BC) has developed only metabolic resistance (enhanced metabolism by esterases), without modification of the insecticide target site (AChE). Development of insecticide resistance was caused by long-term application of acetylcholinesterase inhibitors (organophosphates and carbamates) in these conventional orchards.",
publisher = "Edp Sciences S A, Les Ulis Cedex A",
journal = "Fruits",
title = "Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)",
pages = "142-135",
number = "3",
volume = "70",
doi = "10.1051/fruits/2015005"
}

Tamaš, N., Dojnov, B., Margetić, A., Vujcić, M., Špirović, B., Miletić, N., Stević, M.,& Vujcić, Z.. (2015). Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae). in Fruits
Edp Sciences S A, Les Ulis Cedex A., 70(3), 135-142.
https://doi.org/10.1051/fruits/2015005

Tamaš N, Dojnov B, Margetić A, Vujcić M, Špirović B, Miletić N, Stević M, Vujcić Z. Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae). in Fruits. 2015;70(3):135-142.
doi:10.1051/fruits/2015005 .

Tamaš, Nenad, Dojnov, Biljana, Margetić, Aleksandra, Vujcić, Miroslava, Špirović, Bojana, Miletić, Novica, Stević, Milan, Vujcić, Zoran, "Resistance to common organophosphate and carbamate insecticides in Aphis pomi (Hemiptera: Aphididae)" in Fruits, 70, no. 3 (2015):135-142,
https://doi.org/10.1051/fruits/2015005 . .