TY  - DATA
AU  - Pešić, Miloš P.
AU  - Todorov, Miljana D.
AU  - Drakulić, Branko J.
AU  - Juranić, Ivan O.
AU  - Verbić, Tatjana
AU  - Zloh, Mire
AU  - Cvijetić, Ilija
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3050
PB  - Springer/Plenum Publishers, New York
T2  - Structural Chemistry
T1  - Supplementary material for the article: Cvijetić, I. N.; Pešić, M. P.; Todorov, M. D.; Drakulić, B. J.; Juranić, I. O.; Verbić, T. Ž.; Zloh, M. Tautomerism of 4-Phenyl-2,4-Dioxobutanoic Acid. Insights from PH Ramping NMR Study and Quantum Chemical Calculations. Structural Chemistry 2018, 29 (2), 423–434. https://doi.org/10.1007/s11224-017-1039-3
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3050
ER  - 

@misc{
author = "Pešić, Miloš P. and Todorov, Miljana D. and Drakulić, Branko J. and Juranić, Ivan O. and Verbić, Tatjana and Zloh, Mire and Cvijetić, Ilija",
year = "2018",
publisher = "Springer/Plenum Publishers, New York",
journal = "Structural Chemistry",
title = "Supplementary material for the article: Cvijetić, I. N.; Pešić, M. P.; Todorov, M. D.; Drakulić, B. J.; Juranić, I. O.; Verbić, T. Ž.; Zloh, M. Tautomerism of 4-Phenyl-2,4-Dioxobutanoic Acid. Insights from PH Ramping NMR Study and Quantum Chemical Calculations. Structural Chemistry 2018, 29 (2), 423–434. https://doi.org/10.1007/s11224-017-1039-3",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3050"
}

Pešić, M. P., Todorov, M. D., Drakulić, B. J., Juranić, I. O., Verbić, T., Zloh, M.,& Cvijetić, I.. (2018). Supplementary material for the article: Cvijetić, I. N.; Pešić, M. P.; Todorov, M. D.; Drakulić, B. J.; Juranić, I. O.; Verbić, T. Ž.; Zloh, M. Tautomerism of 4-Phenyl-2,4-Dioxobutanoic Acid. Insights from PH Ramping NMR Study and Quantum Chemical Calculations. Structural Chemistry 2018, 29 (2), 423–434. https://doi.org/10.1007/s11224-017-1039-3. in Structural Chemistry
Springer/Plenum Publishers, New York..
https://hdl.handle.net/21.15107/rcub_cherry_3050

Pešić MP, Todorov MD, Drakulić BJ, Juranić IO, Verbić T, Zloh M, Cvijetić I. Supplementary material for the article: Cvijetić, I. N.; Pešić, M. P.; Todorov, M. D.; Drakulić, B. J.; Juranić, I. O.; Verbić, T. Ž.; Zloh, M. Tautomerism of 4-Phenyl-2,4-Dioxobutanoic Acid. Insights from PH Ramping NMR Study and Quantum Chemical Calculations. Structural Chemistry 2018, 29 (2), 423–434. https://doi.org/10.1007/s11224-017-1039-3. in Structural Chemistry. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3050 .

Pešić, Miloš P., Todorov, Miljana D., Drakulić, Branko J., Juranić, Ivan O., Verbić, Tatjana, Zloh, Mire, Cvijetić, Ilija, "Supplementary material for the article: Cvijetić, I. N.; Pešić, M. P.; Todorov, M. D.; Drakulić, B. J.; Juranić, I. O.; Verbić, T. Ž.; Zloh, M. Tautomerism of 4-Phenyl-2,4-Dioxobutanoic Acid. Insights from PH Ramping NMR Study and Quantum Chemical Calculations. Structural Chemistry 2018, 29 (2), 423–434. https://doi.org/10.1007/s11224-017-1039-3" in Structural Chemistry (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3050 .

TY  - DATA
AU  - Cvijetić, Ilija
AU  - Verbić, Tatjana
AU  - de Resende, Pedro Ernesto
AU  - Stapleton, Paul
AU  - Gibbons, Simon
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
AU  - Zloh, Mire
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3195
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux
T2  - European Journal of Medicinal Chemistry
T1  - Supplementary material for the article: Cvijetić, I. N.; Verbić, T. Ž.; Ernesto de Resende, P.; Stapleton, P.; Gibbons, S.; Juranić, I.  O.; Drakulić, B. J.; Zloh, M. Design, Synthesis and Biological Evaluation of Novel  Aryldiketo Acids with Enhanced Antibacterial Activity against Multidrug Resistant Bacterial  Strains. European Journal of Medicinal Chemistry 2018, 143, 1474–1488.  https://doi.org/10.1016/j.ejmech.2017.10.045
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3195
ER  - 

@misc{
author = "Cvijetić, Ilija and Verbić, Tatjana and de Resende, Pedro Ernesto and Stapleton, Paul and Gibbons, Simon and Juranić, Ivan O. and Drakulić, Branko J. and Zloh, Mire",
year = "2018",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux",
journal = "European Journal of Medicinal Chemistry",
title = "Supplementary material for the article: Cvijetić, I. N.; Verbić, T. Ž.; Ernesto de Resende, P.; Stapleton, P.; Gibbons, S.; Juranić, I.  O.; Drakulić, B. J.; Zloh, M. Design, Synthesis and Biological Evaluation of Novel  Aryldiketo Acids with Enhanced Antibacterial Activity against Multidrug Resistant Bacterial  Strains. European Journal of Medicinal Chemistry 2018, 143, 1474–1488.  https://doi.org/10.1016/j.ejmech.2017.10.045",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3195"
}

Cvijetić, I., Verbić, T., de Resende, P. E., Stapleton, P., Gibbons, S., Juranić, I. O., Drakulić, B. J.,& Zloh, M.. (2018). Supplementary material for the article: Cvijetić, I. N.; Verbić, T. Ž.; Ernesto de Resende, P.; Stapleton, P.; Gibbons, S.; Juranić, I.  O.; Drakulić, B. J.; Zloh, M. Design, Synthesis and Biological Evaluation of Novel  Aryldiketo Acids with Enhanced Antibacterial Activity against Multidrug Resistant Bacterial  Strains. European Journal of Medicinal Chemistry 2018, 143, 1474–1488.  https://doi.org/10.1016/j.ejmech.2017.10.045. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux..
https://hdl.handle.net/21.15107/rcub_cherry_3195

Cvijetić I, Verbić T, de Resende PE, Stapleton P, Gibbons S, Juranić IO, Drakulić BJ, Zloh M. Supplementary material for the article: Cvijetić, I. N.; Verbić, T. Ž.; Ernesto de Resende, P.; Stapleton, P.; Gibbons, S.; Juranić, I.  O.; Drakulić, B. J.; Zloh, M. Design, Synthesis and Biological Evaluation of Novel  Aryldiketo Acids with Enhanced Antibacterial Activity against Multidrug Resistant Bacterial  Strains. European Journal of Medicinal Chemistry 2018, 143, 1474–1488.  https://doi.org/10.1016/j.ejmech.2017.10.045. in European Journal of Medicinal Chemistry. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3195 .

Cvijetić, Ilija, Verbić, Tatjana, de Resende, Pedro Ernesto, Stapleton, Paul, Gibbons, Simon, Juranić, Ivan O., Drakulić, Branko J., Zloh, Mire, "Supplementary material for the article: Cvijetić, I. N.; Verbić, T. Ž.; Ernesto de Resende, P.; Stapleton, P.; Gibbons, S.; Juranić, I.  O.; Drakulić, B. J.; Zloh, M. Design, Synthesis and Biological Evaluation of Novel  Aryldiketo Acids with Enhanced Antibacterial Activity against Multidrug Resistant Bacterial  Strains. European Journal of Medicinal Chemistry 2018, 143, 1474–1488.  https://doi.org/10.1016/j.ejmech.2017.10.045" in European Journal of Medicinal Chemistry (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3195 .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Pešić, Miloš P.
AU  - Todorov, Miljana D.
AU  - Drakulić, Branko J.
AU  - Juranić, Ivan O.
AU  - Verbić, Tatjana
AU  - Zloh, Mire
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2111
AB  - Aryldiketo acids (ADKs) exhibit the variety of biological activities, mainly due to large affinity toward divalent metal ions. Metal complexation ability of ADKs, as well as interactions with proteins, depend on tautomeric form present in solution. The main aim of this study was to fully explore the tautomeric preferences of 4-phenyl-2,4-dioxobutanoic acid (4PDA), as ADKs representative, in aqueous media at different pH values. 1D and 2D NMR spectroscopy in combination with quantum chemical calculations was applied in order to better understand the tautomeric preferences of 4PDA. The data in highly acidic media are especially interesting since there are no such findings in the literature due to low solubility of ADKs in molecular form. At low pH values, where 4PDA is unionized, the most abundant tautomeric form is enol with keto group closer to phenyl ring. At higher pH values, mixture of two 4PDA ionic forms coexists in solution. Their ratio calculated according to NMR data fits the values predicted using two experimentally determined pK (a) values. Based on the complexity of H-1 NMR spectrum of monoanionic 4PDA form, coexistence of two stable rotamers was assumed. In an alkaline media, 4PDA is mostly present in dianionic form. As pi-electrons of dianion are delocalized over an entire keto-enol moiety, spectral distinction between tautomers was not possible. Quantum chemical calculations were used to predict relative stability of tautomers. The predictions were in good accordance with experimental results only in case when explicit water molecule was included in calculations.
PB  - Springer/Plenum Publishers, New York
T2  - Structural Chemistry
T1  - Tautomerism of 4-phenyl-2,4-dioxobutanoic acid. Insights from pH ramping NMR study and quantum chemical calculations
VL  - 29
IS  - 2
SP  - 423
EP  - 434
DO  - 10.1007/s11224-017-1039-3
ER  - 

@article{
author = "Cvijetić, Ilija and Pešić, Miloš P. and Todorov, Miljana D. and Drakulić, Branko J. and Juranić, Ivan O. and Verbić, Tatjana and Zloh, Mire",
year = "2018",
abstract = "Aryldiketo acids (ADKs) exhibit the variety of biological activities, mainly due to large affinity toward divalent metal ions. Metal complexation ability of ADKs, as well as interactions with proteins, depend on tautomeric form present in solution. The main aim of this study was to fully explore the tautomeric preferences of 4-phenyl-2,4-dioxobutanoic acid (4PDA), as ADKs representative, in aqueous media at different pH values. 1D and 2D NMR spectroscopy in combination with quantum chemical calculations was applied in order to better understand the tautomeric preferences of 4PDA. The data in highly acidic media are especially interesting since there are no such findings in the literature due to low solubility of ADKs in molecular form. At low pH values, where 4PDA is unionized, the most abundant tautomeric form is enol with keto group closer to phenyl ring. At higher pH values, mixture of two 4PDA ionic forms coexists in solution. Their ratio calculated according to NMR data fits the values predicted using two experimentally determined pK (a) values. Based on the complexity of H-1 NMR spectrum of monoanionic 4PDA form, coexistence of two stable rotamers was assumed. In an alkaline media, 4PDA is mostly present in dianionic form. As pi-electrons of dianion are delocalized over an entire keto-enol moiety, spectral distinction between tautomers was not possible. Quantum chemical calculations were used to predict relative stability of tautomers. The predictions were in good accordance with experimental results only in case when explicit water molecule was included in calculations.",
publisher = "Springer/Plenum Publishers, New York",
journal = "Structural Chemistry",
title = "Tautomerism of 4-phenyl-2,4-dioxobutanoic acid. Insights from pH ramping NMR study and quantum chemical calculations",
volume = "29",
number = "2",
pages = "423-434",
doi = "10.1007/s11224-017-1039-3"
}

Cvijetić, I., Pešić, M. P., Todorov, M. D., Drakulić, B. J., Juranić, I. O., Verbić, T.,& Zloh, M.. (2018). Tautomerism of 4-phenyl-2,4-dioxobutanoic acid. Insights from pH ramping NMR study and quantum chemical calculations. in Structural Chemistry
Springer/Plenum Publishers, New York., 29(2), 423-434.
https://doi.org/10.1007/s11224-017-1039-3

Cvijetić I, Pešić MP, Todorov MD, Drakulić BJ, Juranić IO, Verbić T, Zloh M. Tautomerism of 4-phenyl-2,4-dioxobutanoic acid. Insights from pH ramping NMR study and quantum chemical calculations. in Structural Chemistry. 2018;29(2):423-434.
doi:10.1007/s11224-017-1039-3 .

Cvijetić, Ilija, Pešić, Miloš P., Todorov, Miljana D., Drakulić, Branko J., Juranić, Ivan O., Verbić, Tatjana, Zloh, Mire, "Tautomerism of 4-phenyl-2,4-dioxobutanoic acid. Insights from pH ramping NMR study and quantum chemical calculations" in Structural Chemistry, 29, no. 2 (2018):423-434,
https://doi.org/10.1007/s11224-017-1039-3 . .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Verbić, Tatjana
AU  - de Resende, Pedro Ernesto
AU  - Stapleton, Paul
AU  - Gibbons, Simon
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
AU  - Zloh, Mire
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2075
AB  - Antimicrobial resistance (AMR) is a major health problem worldwide, because of ability of bacteria, fungi and viruses to evade known therapeutic agents used in treatment of infections. Aryldiketo acids (ADK) have shown antimicrobial activity against several resistant strains including Gram-positive Staphylococcus aureus bacteria. Our previous studies revealed that ADK analogues having bulky alkyl group in ortho position on a phenyl ring have up to ten times better activity than norfloxacin against the same strains. Rational modifications of analogues by introduction of hydrophobic substituents on the aromatic ring has led to more than tenfold increase in antibacterial activity against multidrug resistant Gram positive strains. To elucidate a potential mechanism of action for this potentially novel class of antimicrobials, several bacterial enzymes were identified as putative targets according to literature data and pharmacophoric similarity searches for potent ADK analogues. Among the seven bacterial targets chosen, the strongest favorable binding interactions were observed between most active analogue and S. aureus dehydrosqualene synthase and DNA gyrase. Furthermore, the docking results in combination with literature data suggest that these novel molecules could also target several other bacterial enzymes, including prenyl-transferases and methionine aminopeptidase. These results and our statistically significant 3D QSAR model could be used to guide the further design of more potent derivatives as well as in virtual screening for novel antibacterial agents. (C) 2017 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux
T2  - European Journal of Medicinal Chemistry
T1  - Design, synthesis and biological evaluation of novel aryldiketo acids with enhanced antibacterial activity against multidrug resistant bacterial strains
VL  - 143
SP  - 1474
EP  - 1488
DO  - 10.1016/j.ejmech.2017.10.045
ER  - 

@article{
author = "Cvijetić, Ilija and Verbić, Tatjana and de Resende, Pedro Ernesto and Stapleton, Paul and Gibbons, Simon and Juranić, Ivan O. and Drakulić, Branko J. and Zloh, Mire",
year = "2018",
abstract = "Antimicrobial resistance (AMR) is a major health problem worldwide, because of ability of bacteria, fungi and viruses to evade known therapeutic agents used in treatment of infections. Aryldiketo acids (ADK) have shown antimicrobial activity against several resistant strains including Gram-positive Staphylococcus aureus bacteria. Our previous studies revealed that ADK analogues having bulky alkyl group in ortho position on a phenyl ring have up to ten times better activity than norfloxacin against the same strains. Rational modifications of analogues by introduction of hydrophobic substituents on the aromatic ring has led to more than tenfold increase in antibacterial activity against multidrug resistant Gram positive strains. To elucidate a potential mechanism of action for this potentially novel class of antimicrobials, several bacterial enzymes were identified as putative targets according to literature data and pharmacophoric similarity searches for potent ADK analogues. Among the seven bacterial targets chosen, the strongest favorable binding interactions were observed between most active analogue and S. aureus dehydrosqualene synthase and DNA gyrase. Furthermore, the docking results in combination with literature data suggest that these novel molecules could also target several other bacterial enzymes, including prenyl-transferases and methionine aminopeptidase. These results and our statistically significant 3D QSAR model could be used to guide the further design of more potent derivatives as well as in virtual screening for novel antibacterial agents. (C) 2017 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux",
journal = "European Journal of Medicinal Chemistry",
title = "Design, synthesis and biological evaluation of novel aryldiketo acids with enhanced antibacterial activity against multidrug resistant bacterial strains",
volume = "143",
pages = "1474-1488",
doi = "10.1016/j.ejmech.2017.10.045"
}

Cvijetić, I., Verbić, T., de Resende, P. E., Stapleton, P., Gibbons, S., Juranić, I. O., Drakulić, B. J.,& Zloh, M.. (2018). Design, synthesis and biological evaluation of novel aryldiketo acids with enhanced antibacterial activity against multidrug resistant bacterial strains. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Issy-Les-Moulineaux., 143, 1474-1488.
https://doi.org/10.1016/j.ejmech.2017.10.045

Cvijetić I, Verbić T, de Resende PE, Stapleton P, Gibbons S, Juranić IO, Drakulić BJ, Zloh M. Design, synthesis and biological evaluation of novel aryldiketo acids with enhanced antibacterial activity against multidrug resistant bacterial strains. in European Journal of Medicinal Chemistry. 2018;143:1474-1488.
doi:10.1016/j.ejmech.2017.10.045 .

Cvijetić, Ilija, Verbić, Tatjana, de Resende, Pedro Ernesto, Stapleton, Paul, Gibbons, Simon, Juranić, Ivan O., Drakulić, Branko J., Zloh, Mire, "Design, synthesis and biological evaluation of novel aryldiketo acids with enhanced antibacterial activity against multidrug resistant bacterial strains" in European Journal of Medicinal Chemistry, 143 (2018):1474-1488,
https://doi.org/10.1016/j.ejmech.2017.10.045 . .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2384
AB  - Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana N. and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "Background: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A. N., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić AN, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana N., Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta: General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Nikolić, Jasna
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Đorđević, Neda O.
AU  - Anđelković, Uroš
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2384
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2954
AB  - ackground: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells
VL  - 1861
IS  - 2
SP  - 126
EP  - 134
DO  - 10.1016/j.bbagen.2016.11.021
ER  - 

@article{
author = "Nikolić, Jasna and Nešić, Andrijana N. and Čavić, Milena and Đorđević, Neda O. and Anđelković, Uroš and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "ackground: Protein oxidation can occur as a consequence of lipid peroxidation during food processing. The aim of this work was to explore the effect of malondialdehyde (MDA) modification of ovalbumin (OVA) on its interaction with T84 intestinal cells. Methods: Molecular dynamics simulation was employed for the prediction of MDA modification in the OVA, while introduced structural changes were evaluated by measurement of carbonyl group content, fluorescence spectra, MS/MS analysis, and IgE reactivity. Effects of MDA modified OVA on T84 epithelial cells were analyzed by gene expression for pro-inflammatory cytokines and protein secretion. Results: Out of 9 predicted, five modified Lys residues were confirmed by MS/MS analysis: (51)TQINKVVR(58), (85)DILNQITKPNDVYSFSLASR(104), (111)YPILPEYLQCVKELYR(126), (187)AFKDEDTQAMPFR(99), (KIKVYLPR284)-K-277, and (IKVYLPR284)-I-278. The introduced MDA modifications influenced profile of IgE reactivity to OVA. Treatment of T84 epithelial cells with OVA and OVA modified with 1 mM MDA, induced up-regulation of pro-inflammatory cytokines (IL-1 beta,IL-25, IL-33, TSLP and TNF alpha), while OVA modification with 10 mM MDA induced down regulation of the cytokine expression profile, except for IL-1 beta. OVA and OVA modified with 1 mM MDA induced secretion of epithelial cells specific cytokine IL-33. Conclusions: This finding indicated that OVA and its MDA modified form have the potential to trigger the innate immunity by inducing up-regulation and secretion of pro-allergenic IL-33 in T84 intestinal epithelial cells. General significance: Interactions of ovalbumin and its MDA modified form with intestinal epithelial cells can induce a specific immunological priming necessary for the downstream activation of innate immunity. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells",
volume = "1861",
number = "2",
pages = "126-134",
doi = "10.1016/j.bbagen.2016.11.021"
}

Nikolić, J., Nešić, A. N., Čavić, M., Đorđević, N. O., Anđelković, U., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1861(2), 126-134.
https://doi.org/10.1016/j.bbagen.2016.11.021

Nikolić J, Nešić AN, Čavić M, Đorđević NO, Anđelković U, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells. in Biochimica et Biophysica Acta: General Subjects. 2017;1861(2):126-134.
doi:10.1016/j.bbagen.2016.11.021 .

Nikolić, Jasna, Nešić, Andrijana N., Čavić, Milena, Đorđević, Neda O., Anđelković, Uroš, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Effect of malondialdehyde on the ovalbumin structure and its interactions with T84 epithelial cells" in Biochimica et Biophysica Acta: General Subjects, 1861, no. 2 (2017):126-134,
https://doi.org/10.1016/j.bbagen.2016.11.021 . .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Verbić, Tatjana
AU  - Drakulić, Branko J.
AU  - Stanković, Dalibor
AU  - Juranić, Ivan O.
AU  - Manojlović, Dragan D.
AU  - Zloh, Mire
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2458
AB  - Redox properties of a set of aryldiketo acids (ADKs), small organic molecules that comprise 2,4-dioxobutanoic acid moiety, were studied. Along with well-known HIV-1 integrase (IN) inhibition, ADKs exert widespread biological activities. The aim of this work was to evaluate the effects of aryl substitutions on the properties of the dioxobutanoic moiety that is involved in key interactions with metal ions within the active sites of target enzymes. The effect of pH on the electronic properties of nine congeners was examined using cyclic voltammetry and differential pulse polarography. The compounds were chosen as a simple set of congeners bearing Me-groups on the phenyl ring, which should not be involved in electrochemical reactions, leaving the diketo moiety as the sole electrophore. The substitution pattern was systematically varied, yielding a set having different torsion between the phenyl ring and the aryl keto group (Ar-C(O)). The protonation state of the ADKs at different pH values was determined from the experimentally obtained pK(a) values. The results showed that an equal number of protons and electrons were involved in the oxidation and reduction reactions at the surface of the electrode. Quantitative linear correlations were found between the reduction potentials and the energies of the frontier orbitals, calculated for neutral, mono-anionic and the corresponding radical anionic species, and the steric parameter as two independent variables.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Redox properties of alkyl-substituted 4-aryl-2,4-dioxobutanoic acids
VL  - 82
IS  - 3
SP  - 303
EP  - 316
DO  - 10.2298/JSC161118021C
ER  - 

@article{
author = "Cvijetić, Ilija and Verbić, Tatjana and Drakulić, Branko J. and Stanković, Dalibor and Juranić, Ivan O. and Manojlović, Dragan D. and Zloh, Mire",
year = "2017",
abstract = "Redox properties of a set of aryldiketo acids (ADKs), small organic molecules that comprise 2,4-dioxobutanoic acid moiety, were studied. Along with well-known HIV-1 integrase (IN) inhibition, ADKs exert widespread biological activities. The aim of this work was to evaluate the effects of aryl substitutions on the properties of the dioxobutanoic moiety that is involved in key interactions with metal ions within the active sites of target enzymes. The effect of pH on the electronic properties of nine congeners was examined using cyclic voltammetry and differential pulse polarography. The compounds were chosen as a simple set of congeners bearing Me-groups on the phenyl ring, which should not be involved in electrochemical reactions, leaving the diketo moiety as the sole electrophore. The substitution pattern was systematically varied, yielding a set having different torsion between the phenyl ring and the aryl keto group (Ar-C(O)). The protonation state of the ADKs at different pH values was determined from the experimentally obtained pK(a) values. The results showed that an equal number of protons and electrons were involved in the oxidation and reduction reactions at the surface of the electrode. Quantitative linear correlations were found between the reduction potentials and the energies of the frontier orbitals, calculated for neutral, mono-anionic and the corresponding radical anionic species, and the steric parameter as two independent variables.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Redox properties of alkyl-substituted 4-aryl-2,4-dioxobutanoic acids",
volume = "82",
number = "3",
pages = "303-316",
doi = "10.2298/JSC161118021C"
}

Cvijetić, I., Verbić, T., Drakulić, B. J., Stanković, D., Juranić, I. O., Manojlović, D. D.,& Zloh, M.. (2017). Redox properties of alkyl-substituted 4-aryl-2,4-dioxobutanoic acids. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 82(3), 303-316.
https://doi.org/10.2298/JSC161118021C

Cvijetić I, Verbić T, Drakulić BJ, Stanković D, Juranić IO, Manojlović DD, Zloh M. Redox properties of alkyl-substituted 4-aryl-2,4-dioxobutanoic acids. in Journal of the Serbian Chemical Society. 2017;82(3):303-316.
doi:10.2298/JSC161118021C .

Cvijetić, Ilija, Verbić, Tatjana, Drakulić, Branko J., Stanković, Dalibor, Juranić, Ivan O., Manojlović, Dragan D., Zloh, Mire, "Redox properties of alkyl-substituted 4-aryl-2,4-dioxobutanoic acids" in Journal of the Serbian Chemical Society, 82, no. 3 (2017):303-316,
https://doi.org/10.2298/JSC161118021C . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Bulat, Tanja
AU  - Aradska, Jana
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2472
AB  - BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera
VL  - 92
IS  - 6
SP  - 1328
EP  - 1335
DO  - 10.1002/jctb.5127
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Bulat, Tanja and Aradska, Jana and Atanasković-Marković, Marina and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera",
volume = "92",
number = "6",
pages = "1328-1335",
doi = "10.1002/jctb.5127"
}

Mrkić, I., Minić, R., Bulat, T., Aradska, J., Atanasković-Marković, M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2017). Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology
Wiley, Hoboken., 92(6), 1328-1335.
https://doi.org/10.1002/jctb.5127

Mrkić I, Minić R, Bulat T, Aradska J, Atanasković-Marković M, Drakulić BJ, Gavrović-Jankulović M. Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology. 2017;92(6):1328-1335.
doi:10.1002/jctb.5127 .

Mrkić, Ivan, Minić, Rajna, Bulat, Tanja, Aradska, Jana, Atanasković-Marković, Marina, Drakulić, Branko J., Gavrović-Jankulović, Marija, "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera" in Journal of Chemical Technology and Biotechnology, 92, no. 6 (2017):1328-1335,
https://doi.org/10.1002/jctb.5127 . .

TY  - JOUR
AU  - Trbojević-Ivić, Jovana
AU  - Dimitrijević, Aleksandra
AU  - Milosavić, Nenad
AU  - Bezbradica, Dejan
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
AU  - Pavlović, Marija
AU  - Rogniaux, Helene
AU  - Veličković, Dušan
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1914
AB  - Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling
VL  - 6
IS  - 41
SP  - 34818
EP  - 34824
DO  - 10.1039/c6ra07521e
ER  - 

@article{
author = "Trbojević-Ivić, Jovana and Dimitrijević, Aleksandra and Milosavić, Nenad and Bezbradica, Dejan and Drakulić, Branko J. and Gavrović-Jankulović, Marija and Pavlović, Marija and Rogniaux, Helene and Veličković, Dušan",
year = "2016",
abstract = "Hydroxyapatite (HAP), a calcium-phosphate bioactive ceramic, is actively employed in medical and separation sciences. Although different classes of biomacromolecules interact with this material, interactions with proteins are the most important, since they directly affect the biocompatibility of the carrier and it's industrial application. In the presented work, we thoroughly investigate and elucidate the interaction mechanism between Candida rugosa lipase (CRL) upon it's immobilization on HAP, since this immobilized enzyme showed advanced catalytic properties in previous studies. Applying elution and protein modification strategies we concluded that Ca-chelation of HAP's C-site and CRL's -COOH groups is the most probable interacting mechanism. A proteomics approach revealed that this chelation is conserved throughout all CRL isoforms, while results of molecular modelling led us to propose the involvement of a specific region of the protein surface and side chains in interactions with HAP.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling",
volume = "6",
number = "41",
pages = "34818-34824",
doi = "10.1039/c6ra07521e"
}

Trbojević-Ivić, J., Dimitrijević, A., Milosavić, N., Bezbradica, D., Drakulić, B. J., Gavrović-Jankulović, M., Pavlović, M., Rogniaux, H.,& Veličković, D.. (2016). Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(41), 34818-34824.
https://doi.org/10.1039/c6ra07521e

Trbojević-Ivić J, Dimitrijević A, Milosavić N, Bezbradica D, Drakulić BJ, Gavrović-Jankulović M, Pavlović M, Rogniaux H, Veličković D. Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling. in RSC Advances. 2016;6(41):34818-34824.
doi:10.1039/c6ra07521e .

Trbojević-Ivić, Jovana, Dimitrijević, Aleksandra, Milosavić, Nenad, Bezbradica, Dejan, Drakulić, Branko J., Gavrović-Jankulović, Marija, Pavlović, Marija, Rogniaux, Helene, Veličković, Dušan, "Assessment of the interacting mechanism between Candida rugosa lipases and hydroxyapatite and identification of the hydroxyapatite-binding sequence through proteomics and molecular modelling" in RSC Advances, 6, no. 41 (2016):34818-34824,
https://doi.org/10.1039/c6ra07521e . .

TY  - DATA
AU  - Cvijetić, Ilija
AU  - Tanç, Muhammet
AU  - Juranić, Ivan O.
AU  - Verbić, Tatjana
AU  - Supuran, Claudiu T.
AU  - Drakulić, Branko J.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3328
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Bioorganic and Medicinal Chemistry
T1  - Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3328
ER  - 

@misc{
author = "Cvijetić, Ilija and Tanç, Muhammet and Juranić, Ivan O. and Verbić, Tatjana and Supuran, Claudiu T. and Drakulić, Branko J.",
year = "2015",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Bioorganic and Medicinal Chemistry",
title = "Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3328"
}

Cvijetić, I., Tanç, M., Juranić, I. O., Verbić, T., Supuran, C. T.,& Drakulić, B. J.. (2015). Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052. in Bioorganic and Medicinal Chemistry
Pergamon-Elsevier Science Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3328

Cvijetić I, Tanç M, Juranić IO, Verbić T, Supuran CT, Drakulić BJ. Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052. in Bioorganic and Medicinal Chemistry. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3328 .

Cvijetić, Ilija, Tanç, Muhammet, Juranić, Ivan O., Verbić, Tatjana, Supuran, Claudiu T., Drakulić, Branko J., "Supplementary data for the article: Cvijetić, I. N.; Tanç, M.; Juranić, I. O.; Verbić, T. Ž.; Supuran, C. T.; Drakulić, B. J. 5-Aryl-1H-Pyrazole-3-Carboxylic Acids as Selective Inhibitors of Human Carbonic Anhydrases IX and XII. Bioorganic and Medicinal Chemistry 2015, 23 (15), 4649–4659. https://doi.org/10.1016/j.bmc.2015.05.052" in Bioorganic and Medicinal Chemistry (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3328 .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Tanç, Muhammet
AU  - Juranić, Ivan O.
AU  - Verbić, Tatjana
AU  - Supuran, Claudiu T.
AU  - Drakulić, Branko J.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3327
AB  - Inhibitory activity of a congeneric set of 23 phenyl-substituted 5-phenyl-pyrazole-3-carboxylic acids toward human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II, IX and XII was evaluated by a stopped-flow CO2 hydrase assay. These compounds exerted a clear, selective inhibition of hCA IX and XII over hCAI and II, with Ki in two to one digit micromolar concentrations (4-50 mu M). Derivatives bearing bulkier substituents in para-position of the phenyl ring inhibited hCA XII at one-digit micromolar concentrations, while derivatives having alkyl substituents in both ortho-and meta-positions inhibited hCA IX with Kis ranging between 5 and 25 mu M. Results of docking experiments offered a rational explanation on the selectivity of these compounds toward CA IX and XII, as well as on the substitution patterns leading to best CA IX or CA XII inhibitors. By examining the active sites of these four isoforms with GRID generated molecular-interaction fields, striking differences between hCA XII and the other three isoforms were observed. The field of hydrophobic probe (DRY) appeared significantly different in CA XII active site, comparing to other three isoforms studied. To the best of our knowledge such an observation was not reported in literature so far. Considering the selectivity of these carboxylates towards membrane-associated over cytosolic CA isoforms, the title compounds could be useful for the development of isoform-specific non-sulfonamide CA inhibitors.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Bioorganic and Medicinal Chemistry
T1  - 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII
VL  - 23
IS  - 15
SP  - 4649
EP  - 4659
DO  - 10.1016/j.bmc.2015.05.052
ER  - 

@article{
author = "Cvijetić, Ilija and Tanç, Muhammet and Juranić, Ivan O. and Verbić, Tatjana and Supuran, Claudiu T. and Drakulić, Branko J.",
year = "2015",
abstract = "Inhibitory activity of a congeneric set of 23 phenyl-substituted 5-phenyl-pyrazole-3-carboxylic acids toward human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II, IX and XII was evaluated by a stopped-flow CO2 hydrase assay. These compounds exerted a clear, selective inhibition of hCA IX and XII over hCAI and II, with Ki in two to one digit micromolar concentrations (4-50 mu M). Derivatives bearing bulkier substituents in para-position of the phenyl ring inhibited hCA XII at one-digit micromolar concentrations, while derivatives having alkyl substituents in both ortho-and meta-positions inhibited hCA IX with Kis ranging between 5 and 25 mu M. Results of docking experiments offered a rational explanation on the selectivity of these compounds toward CA IX and XII, as well as on the substitution patterns leading to best CA IX or CA XII inhibitors. By examining the active sites of these four isoforms with GRID generated molecular-interaction fields, striking differences between hCA XII and the other three isoforms were observed. The field of hydrophobic probe (DRY) appeared significantly different in CA XII active site, comparing to other three isoforms studied. To the best of our knowledge such an observation was not reported in literature so far. Considering the selectivity of these carboxylates towards membrane-associated over cytosolic CA isoforms, the title compounds could be useful for the development of isoform-specific non-sulfonamide CA inhibitors.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Bioorganic and Medicinal Chemistry",
title = "5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII",
volume = "23",
number = "15",
pages = "4649-4659",
doi = "10.1016/j.bmc.2015.05.052"
}

Cvijetić, I., Tanç, M., Juranić, I. O., Verbić, T., Supuran, C. T.,& Drakulić, B. J.. (2015). 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII. in Bioorganic and Medicinal Chemistry
Pergamon-Elsevier Science Ltd, Oxford., 23(15), 4649-4659.
https://doi.org/10.1016/j.bmc.2015.05.052

Cvijetić I, Tanç M, Juranić IO, Verbić T, Supuran CT, Drakulić BJ. 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII. in Bioorganic and Medicinal Chemistry. 2015;23(15):4649-4659.
doi:10.1016/j.bmc.2015.05.052 .

Cvijetić, Ilija, Tanç, Muhammet, Juranić, Ivan O., Verbić, Tatjana, Supuran, Claudiu T., Drakulić, Branko J., "5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII" in Bioorganic and Medicinal Chemistry, 23, no. 15 (2015):4649-4659,
https://doi.org/10.1016/j.bmc.2015.05.052 . .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Tanç, Muhammet
AU  - Juranić, Ivan O.
AU  - Verbić, Tatjana
AU  - Supuran, Claudiu T.
AU  - Drakulić, Branko J.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1742
AB  - Inhibitory activity of a congeneric set of 23 phenyl-substituted 5-phenyl-pyrazole-3-carboxylic acids toward human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II, IX and XII was evaluated by a stopped-flow CO2 hydrase assay. These compounds exerted a clear, selective inhibition of hCA IX and XII over hCAI and II, with Ki in two to one digit micromolar concentrations (4-50 mu M). Derivatives bearing bulkier substituents in para-position of the phenyl ring inhibited hCA XII at one-digit micromolar concentrations, while derivatives having alkyl substituents in both ortho-and meta-positions inhibited hCA IX with Kis ranging between 5 and 25 mu M. Results of docking experiments offered a rational explanation on the selectivity of these compounds toward CA IX and XII, as well as on the substitution patterns leading to best CA IX or CA XII inhibitors. By examining the active sites of these four isoforms with GRID generated molecular-interaction fields, striking differences between hCA XII and the other three isoforms were observed. The field of hydrophobic probe (DRY) appeared significantly different in CA XII active site, comparing to other three isoforms studied. To the best of our knowledge such an observation was not reported in literature so far. Considering the selectivity of these carboxylates towards membrane-associated over cytosolic CA isoforms, the title compounds could be useful for the development of isoform-specific non-sulfonamide CA inhibitors.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Bioorganic and Medicinal Chemistry
T1  - 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII
VL  - 23
IS  - 15
SP  - 4649
EP  - 4659
DO  - 10.1016/j.bmc.2015.05.052
ER  - 

@article{
author = "Cvijetić, Ilija and Tanç, Muhammet and Juranić, Ivan O. and Verbić, Tatjana and Supuran, Claudiu T. and Drakulić, Branko J.",
year = "2015",
abstract = "Inhibitory activity of a congeneric set of 23 phenyl-substituted 5-phenyl-pyrazole-3-carboxylic acids toward human carbonic anhydrase (hCA, EC 4.2.1.1) isoforms I, II, IX and XII was evaluated by a stopped-flow CO2 hydrase assay. These compounds exerted a clear, selective inhibition of hCA IX and XII over hCAI and II, with Ki in two to one digit micromolar concentrations (4-50 mu M). Derivatives bearing bulkier substituents in para-position of the phenyl ring inhibited hCA XII at one-digit micromolar concentrations, while derivatives having alkyl substituents in both ortho-and meta-positions inhibited hCA IX with Kis ranging between 5 and 25 mu M. Results of docking experiments offered a rational explanation on the selectivity of these compounds toward CA IX and XII, as well as on the substitution patterns leading to best CA IX or CA XII inhibitors. By examining the active sites of these four isoforms with GRID generated molecular-interaction fields, striking differences between hCA XII and the other three isoforms were observed. The field of hydrophobic probe (DRY) appeared significantly different in CA XII active site, comparing to other three isoforms studied. To the best of our knowledge such an observation was not reported in literature so far. Considering the selectivity of these carboxylates towards membrane-associated over cytosolic CA isoforms, the title compounds could be useful for the development of isoform-specific non-sulfonamide CA inhibitors.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Bioorganic and Medicinal Chemistry",
title = "5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII",
volume = "23",
number = "15",
pages = "4649-4659",
doi = "10.1016/j.bmc.2015.05.052"
}

Cvijetić, I., Tanç, M., Juranić, I. O., Verbić, T., Supuran, C. T.,& Drakulić, B. J.. (2015). 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII. in Bioorganic and Medicinal Chemistry
Pergamon-Elsevier Science Ltd, Oxford., 23(15), 4649-4659.
https://doi.org/10.1016/j.bmc.2015.05.052

Cvijetić I, Tanç M, Juranić IO, Verbić T, Supuran CT, Drakulić BJ. 5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII. in Bioorganic and Medicinal Chemistry. 2015;23(15):4649-4659.
doi:10.1016/j.bmc.2015.05.052 .

Cvijetić, Ilija, Tanç, Muhammet, Juranić, Ivan O., Verbić, Tatjana, Supuran, Claudiu T., Drakulić, Branko J., "5-Aryl-1H-pyrazole-3-carboxylic acids as selective inhibitors of human carbonic anhydrases IX and XII" in Bioorganic and Medicinal Chemistry, 23, no. 15 (2015):4649-4659,
https://doi.org/10.1016/j.bmc.2015.05.052 . .

TY  - JOUR
AU  - Vitorović-Todorović, Maja D.
AU  - Koukoulitsa, Catherine
AU  - Juranić, Ivan O.
AU  - Mandić, Ljuba M.
AU  - Drakulić, Branko J.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1808
AB  - Congeneric set of thirty-eight 4-aryl-4-oxo-2-(N-aryl/cycloalkyl)butanamides has been designed, synthesized and evaluated for acetyl- and butyrylcholinesterase inhibitory activity. Structural variations included cycloalkylamino group attached to C2 position of butanoyl moiety, and variation of amido moiety of molecules. Twelve compounds, mostly piperidino and imidazolo derivatives, inhibited AChE in low micromolar range, and were inactive toward BChE. Several N-methylpiperazino derivatives showed inhibition of BChE in low micromolar or submicromolar concentrations, and were inactive toward AChE. Therefore, the nature of the cycloalkylamino moiety governs the AChE/BChE selectivity profile of compounds. The most active AChE inhibitor showed mixed-type inhibition modality, indicating its binding to free enzyme and to enzyme-substrate complex. Thorough docking calculations of the seven most potent AChE inhibitors from the set, showed that the hydrogen bond can be formed between amide -NH- moiety of compounds and -OH group of Tyr 124. The 10 ns unconstrained molecular dynamic simulation of the AChE- compound 18 complex shows that this interaction is the most persistent. This is, probably, the major anchoring point for the binding. (C) 2014 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations
VL  - 81
SP  - 158
EP  - 175
DO  - 10.1016/j.ejmech.2014.05.008
ER  - 

@article{
author = "Vitorović-Todorović, Maja D. and Koukoulitsa, Catherine and Juranić, Ivan O. and Mandić, Ljuba M. and Drakulić, Branko J.",
year = "2014",
abstract = "Congeneric set of thirty-eight 4-aryl-4-oxo-2-(N-aryl/cycloalkyl)butanamides has been designed, synthesized and evaluated for acetyl- and butyrylcholinesterase inhibitory activity. Structural variations included cycloalkylamino group attached to C2 position of butanoyl moiety, and variation of amido moiety of molecules. Twelve compounds, mostly piperidino and imidazolo derivatives, inhibited AChE in low micromolar range, and were inactive toward BChE. Several N-methylpiperazino derivatives showed inhibition of BChE in low micromolar or submicromolar concentrations, and were inactive toward AChE. Therefore, the nature of the cycloalkylamino moiety governs the AChE/BChE selectivity profile of compounds. The most active AChE inhibitor showed mixed-type inhibition modality, indicating its binding to free enzyme and to enzyme-substrate complex. Thorough docking calculations of the seven most potent AChE inhibitors from the set, showed that the hydrogen bond can be formed between amide -NH- moiety of compounds and -OH group of Tyr 124. The 10 ns unconstrained molecular dynamic simulation of the AChE- compound 18 complex shows that this interaction is the most persistent. This is, probably, the major anchoring point for the binding. (C) 2014 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations",
volume = "81",
pages = "158-175",
doi = "10.1016/j.ejmech.2014.05.008"
}

Vitorović-Todorović, M. D., Koukoulitsa, C., Juranić, I. O., Mandić, L. M.,& Drakulić, B. J.. (2014). Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 81, 158-175.
https://doi.org/10.1016/j.ejmech.2014.05.008

Vitorović-Todorović MD, Koukoulitsa C, Juranić IO, Mandić LM, Drakulić BJ. Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations. in European Journal of Medicinal Chemistry. 2014;81:158-175.
doi:10.1016/j.ejmech.2014.05.008 .

Vitorović-Todorović, Maja D., Koukoulitsa, Catherine, Juranić, Ivan O., Mandić, Ljuba M., Drakulić, Branko J., "Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations" in European Journal of Medicinal Chemistry, 81 (2014):158-175,
https://doi.org/10.1016/j.ejmech.2014.05.008 . .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Vitorović-Todorović, Maja D.
AU  - Juranić, Ivan O.
AU  - Nakarada, Dura J.
AU  - Milosavljević, Milica D.
AU  - Drakulić, Branko J.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1816
AB  - Rates of the aza-Michael addition of piperidine and benzylamine to thirteen (E)-4-aryl-4-oxo-2-butenoic acid phenylamides (AACPs) are reported. Progress of the reaction was monitored by UV/Vis spectroscopy. The 2D NMR spectra confirmed regioselectivity of the reactions. Piperidine and benzylamine provide exclusively beta-adducts in respect to the aroyl keto group. Influence of the substituents of the aroyl phenyl ring of AACPs on the rate of the reaction was quantified by Hammett substituent constants, partial atomic charges, and the energies of frontier orbitals. Good correlations between second-order rate constants and the Hammett substituent constants were obtained (r = 0.98, piperidine; r = 0.94, benzylamine) for para-, and meta-, para-substituted derivatives. Best correlations were obtained with the energies of the lowest unoccupied molecular orbitals of compounds, derived from the MP2 level of theory. Calculated UV/Vis spectra of representative AACPs and their Michael adduct with piperidine and benzylamine are in fair agreement with experimentally obtained data.
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid phenylamides with piperidine and benzylamine: kinetic and theoretical study
VL  - 145
IS  - 8
SP  - 1297
EP  - 1306
DO  - 10.1007/s00706-014-1223-8
ER  - 

@article{
author = "Cvijetić, Ilija and Vitorović-Todorović, Maja D. and Juranić, Ivan O. and Nakarada, Dura J. and Milosavljević, Milica D. and Drakulić, Branko J.",
year = "2014",
abstract = "Rates of the aza-Michael addition of piperidine and benzylamine to thirteen (E)-4-aryl-4-oxo-2-butenoic acid phenylamides (AACPs) are reported. Progress of the reaction was monitored by UV/Vis spectroscopy. The 2D NMR spectra confirmed regioselectivity of the reactions. Piperidine and benzylamine provide exclusively beta-adducts in respect to the aroyl keto group. Influence of the substituents of the aroyl phenyl ring of AACPs on the rate of the reaction was quantified by Hammett substituent constants, partial atomic charges, and the energies of frontier orbitals. Good correlations between second-order rate constants and the Hammett substituent constants were obtained (r = 0.98, piperidine; r = 0.94, benzylamine) for para-, and meta-, para-substituted derivatives. Best correlations were obtained with the energies of the lowest unoccupied molecular orbitals of compounds, derived from the MP2 level of theory. Calculated UV/Vis spectra of representative AACPs and their Michael adduct with piperidine and benzylamine are in fair agreement with experimentally obtained data.",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid phenylamides with piperidine and benzylamine: kinetic and theoretical study",
volume = "145",
number = "8",
pages = "1297-1306",
doi = "10.1007/s00706-014-1223-8"
}

Cvijetić, I., Vitorović-Todorović, M. D., Juranić, I. O., Nakarada, D. J., Milosavljević, M. D.,& Drakulić, B. J.. (2014). Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid phenylamides with piperidine and benzylamine: kinetic and theoretical study. in Monatshefte Fur Chemie
Springer Wien, Wien., 145(8), 1297-1306.
https://doi.org/10.1007/s00706-014-1223-8

Cvijetić I, Vitorović-Todorović MD, Juranić IO, Nakarada DJ, Milosavljević MD, Drakulić BJ. Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid phenylamides with piperidine and benzylamine: kinetic and theoretical study. in Monatshefte Fur Chemie. 2014;145(8):1297-1306.
doi:10.1007/s00706-014-1223-8 .

Cvijetić, Ilija, Vitorović-Todorović, Maja D., Juranić, Ivan O., Nakarada, Dura J., Milosavljević, Milica D., Drakulić, Branko J., "Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid phenylamides with piperidine and benzylamine: kinetic and theoretical study" in Monatshefte Fur Chemie, 145, no. 8 (2014):1297-1306,
https://doi.org/10.1007/s00706-014-1223-8 . .

TY  - DATA
AU  - Vitorović-Todorović, Maja D.
AU  - Koukoulitsa, Catherine
AU  - Juranić, Ivan O.
AU  - Mandić, Ljuba M.
AU  - Drakulić, Branko J.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2906
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2906
ER  - 

@misc{
author = "Vitorović-Todorović, Maja D. and Koukoulitsa, Catherine and Juranić, Ivan O. and Mandić, Ljuba M. and Drakulić, Branko J.",
year = "2014",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2906"
}

Vitorović-Todorović, M. D., Koukoulitsa, C., Juranić, I. O., Mandić, L. M.,& Drakulić, B. J.. (2014). Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris..
https://hdl.handle.net/21.15107/rcub_cherry_2906

Vitorović-Todorović MD, Koukoulitsa C, Juranić IO, Mandić LM, Drakulić BJ. Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008. in European Journal of Medicinal Chemistry. 2014;.
https://hdl.handle.net/21.15107/rcub_cherry_2906 .

Vitorović-Todorović, Maja D., Koukoulitsa, Catherine, Juranić, Ivan O., Mandić, Ljuba M., Drakulić, Branko J., "Supplementary data for the article: Vitorović-Todorović, M. D.; Koukoulitsa, C.; Juranić, I. O.; Mandić, L. M.; Drakulić, B. J. Structural Modifications of 4-Aryl-4-Oxo-2-Aminylbutanamides and Their Acetyl- and Butyrylcholinesterase Inhibitory Activity. Investigation of AChE-Ligand Interactions by Docking Calculations and Molecular Dynamics Simulations. European Journal of Medicinal Chemistry 2014, 81, 158–175. https://doi.org/10.1016/j.ejmech.2014.05.008" in European Journal of Medicinal Chemistry (2014),
https://hdl.handle.net/21.15107/rcub_cherry_2906 .

TY  - JOUR
AU  - Vitorović-Todorović, Maja D.
AU  - Koukoulitsa, Catherine
AU  - Juranić, Ivan O.
AU  - Mandić, Ljuba M.
AU  - Drakulić, Branko J.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2907
AB  - Congeneric set of thirty-eight 4-aryl-4-oxo-2-(N-aryl/cycloalkyl)butanamides has been designed, synthesized and evaluated for acetyl- and butyrylcholinesterase inhibitory activity. Structural variations included cycloalkylamino group attached to C2 position of butanoyl moiety, and variation of amido moiety of molecules. Twelve compounds, mostly piperidino and imidazolo derivatives, inhibited AChE in low micromolar range, and were inactive toward BChE. Several N-methylpiperazino derivatives showed inhibition of BChE in low micromolar or submicromolar concentrations, and were inactive toward AChE. Therefore, the nature of the cycloalkylamino moiety governs the AChE/BChE selectivity profile of compounds. The most active AChE inhibitor showed mixed-type inhibition modality, indicating its binding to free enzyme and to enzyme-substrate complex. Thorough docking calculations of the seven most potent AChE inhibitors from the set, showed that the hydrogen bond can be formed between amide -NH- moiety of compounds and -OH group of Tyr 124. The 10 ns unconstrained molecular dynamic simulation of the AChE- compound 18 complex shows that this interaction is the most persistent. This is, probably, the major anchoring point for the binding. (C) 2014 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations
VL  - 81
SP  - 158
EP  - 175
DO  - 10.1016/j.ejmech.2014.05.008
ER  - 

@article{
author = "Vitorović-Todorović, Maja D. and Koukoulitsa, Catherine and Juranić, Ivan O. and Mandić, Ljuba M. and Drakulić, Branko J.",
year = "2014",
abstract = "Congeneric set of thirty-eight 4-aryl-4-oxo-2-(N-aryl/cycloalkyl)butanamides has been designed, synthesized and evaluated for acetyl- and butyrylcholinesterase inhibitory activity. Structural variations included cycloalkylamino group attached to C2 position of butanoyl moiety, and variation of amido moiety of molecules. Twelve compounds, mostly piperidino and imidazolo derivatives, inhibited AChE in low micromolar range, and were inactive toward BChE. Several N-methylpiperazino derivatives showed inhibition of BChE in low micromolar or submicromolar concentrations, and were inactive toward AChE. Therefore, the nature of the cycloalkylamino moiety governs the AChE/BChE selectivity profile of compounds. The most active AChE inhibitor showed mixed-type inhibition modality, indicating its binding to free enzyme and to enzyme-substrate complex. Thorough docking calculations of the seven most potent AChE inhibitors from the set, showed that the hydrogen bond can be formed between amide -NH- moiety of compounds and -OH group of Tyr 124. The 10 ns unconstrained molecular dynamic simulation of the AChE- compound 18 complex shows that this interaction is the most persistent. This is, probably, the major anchoring point for the binding. (C) 2014 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations",
volume = "81",
pages = "158-175",
doi = "10.1016/j.ejmech.2014.05.008"
}

Vitorović-Todorović, M. D., Koukoulitsa, C., Juranić, I. O., Mandić, L. M.,& Drakulić, B. J.. (2014). Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 81, 158-175.
https://doi.org/10.1016/j.ejmech.2014.05.008

Vitorović-Todorović MD, Koukoulitsa C, Juranić IO, Mandić LM, Drakulić BJ. Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations. in European Journal of Medicinal Chemistry. 2014;81:158-175.
doi:10.1016/j.ejmech.2014.05.008 .

Vitorović-Todorović, Maja D., Koukoulitsa, Catherine, Juranić, Ivan O., Mandić, Ljuba M., Drakulić, Branko J., "Structural modifications of 4-aryl-4-oxo-2-aminylbutanamides and their acetyl- and butyrylcholinesterase inhibitory activity. Investigation of AChE-ligand interactions by docking calculations and molecular dynamics simulations" in European Journal of Medicinal Chemistry, 81 (2014):158-175,
https://doi.org/10.1016/j.ejmech.2014.05.008 . .

TY  - CONF
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1955
AB  - Differences in activity and the structural stability under simulated gastric juice conditions of uninhibited and covalently inhibited cysteine protease, isolated from the fruit, were experimentally observed. We employed molecular dynamics simulations of proteins modeled from the similar ones with known 3D structure to explain experimental findings. Simulations were performed with NAMD, using CHARMM force field in explicit solvent model. Conformational changes observed in MD trajectories offer indication on differences in stability of inhibited vs. uninhibited protein on low pH values. Protonation states of the protein side chains, through the non-bonded interactions that stabilize 3D structures, likely, significantly contribute to difference in stability of uninhibited and covalently inhibited protein on low pH values.
PB  - Springer Int Publishing Ag, Cham
T1  - Dynamics of Uninhibited and Covalently Inhibited Cysteine Protease on Non-physiological pH
VL  - 2
SP  - 75
EP  - 82
DO  - 10.1007/978-3-319-01520-0_9
ER  - 

@conference{
author = "Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "Differences in activity and the structural stability under simulated gastric juice conditions of uninhibited and covalently inhibited cysteine protease, isolated from the fruit, were experimentally observed. We employed molecular dynamics simulations of proteins modeled from the similar ones with known 3D structure to explain experimental findings. Simulations were performed with NAMD, using CHARMM force field in explicit solvent model. Conformational changes observed in MD trajectories offer indication on differences in stability of inhibited vs. uninhibited protein on low pH values. Protonation states of the protein side chains, through the non-bonded interactions that stabilize 3D structures, likely, significantly contribute to difference in stability of uninhibited and covalently inhibited protein on low pH values.",
publisher = "Springer Int Publishing Ag, Cham",
title = "Dynamics of Uninhibited and Covalently Inhibited Cysteine Protease on Non-physiological pH",
volume = "2",
pages = "75-82",
doi = "10.1007/978-3-319-01520-0_9"
}

Drakulić, B. J.,& Gavrović-Jankulović, M.. (2014). Dynamics of Uninhibited and Covalently Inhibited Cysteine Protease on Non-physiological pH. 
Springer Int Publishing Ag, Cham., 2, 75-82.
https://doi.org/10.1007/978-3-319-01520-0_9

Drakulić BJ, Gavrović-Jankulović M. Dynamics of Uninhibited and Covalently Inhibited Cysteine Protease on Non-physiological pH. 2014;2:75-82.
doi:10.1007/978-3-319-01520-0_9 .

Drakulić, Branko J., Gavrović-Jankulović, Marija, "Dynamics of Uninhibited and Covalently Inhibited Cysteine Protease on Non-physiological pH", 2 (2014):75-82,
https://doi.org/10.1007/978-3-319-01520-0_9 . .

TY  - DATA
AU  - Cvijetić, Ilija
AU  - Vitorović-Todorović, Maja D.
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3515
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3515
ER  - 

@misc{
author = "Cvijetić, Ilija and Vitorović-Todorović, Maja D. and Juranić, Ivan O. and Drakulić, Branko J.",
year = "2013",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3515"
}

Cvijetić, I., Vitorović-Todorović, M. D., Juranić, I. O.,& Drakulić, B. J.. (2013). Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6. in Monatshefte Fur Chemie
Springer Wien, Wien..
https://hdl.handle.net/21.15107/rcub_cherry_3515

Cvijetić I, Vitorović-Todorović MD, Juranić IO, Drakulić BJ. Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6. in Monatshefte Fur Chemie. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3515 .

Cvijetić, Ilija, Vitorović-Todorović, Maja D., Juranić, Ivan O., Drakulić, Branko J., "Supplementary data for article: Cvijetić, I.; Vitorović-Todorović, M. D.; Juranić, I. O.; Drakulić, B. J. Reactivity of (E)-4-Aryl-4-Oxo-2-Butenoic Acid Arylamides toward 2-Mercaptoethanol. A LFER Study. Monatshefte Fur Chemie 2013, 144 (12), 1815–1824. https://doi.org/10.1007/s00706-013-1084-6" in Monatshefte Fur Chemie (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3515 .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Vitorović-Todorović, Maja D.
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1441
AB  - The reactivity of fifteen (E)-4-aryl-4-oxo-2-butenoic (aroylacrylic) acid arylamides toward thiols was studied, measuring the rate constants of the addition of model thiol nucleophile, 2-mercaptoethanol. The influence of the variation of the substituents on the phenyl rings on the rate of reaction was quantified using the Hammett substituent constants and descriptors derived from ab initio or semiempirical calculations (atomic charges, HOMO, and LUMO). Statistically significant linear correlations between second-order rate constants and Hammett substituent constants, as well as energies of LUMO orbitals, were obtained. Substituents on both aroyl and arylamido moieties were shown to influence the reactivity of studied compounds toward thiols. The regioselectivity of reaction was confirmed by NMR spectroscopy. Exclusively beta-addition product with respect to the aroyl keto group was obtained. The determined enthalpy and entropy of activation were found to be in agreement with the proposed reaction mechanism, which includes a highly ordered transition state.
PB  - Springer Wien, Wien
T2  - Monatshefte Fur Chemie
T1  - Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid arylamides toward 2-mercaptoethanol. A LFER study
VL  - 144
IS  - 12
SP  - 1815
EP  - 1824
DO  - 10.1007/s00706-013-1084-6
ER  - 

@article{
author = "Cvijetić, Ilija and Vitorović-Todorović, Maja D. and Juranić, Ivan O. and Drakulić, Branko J.",
year = "2013",
abstract = "The reactivity of fifteen (E)-4-aryl-4-oxo-2-butenoic (aroylacrylic) acid arylamides toward thiols was studied, measuring the rate constants of the addition of model thiol nucleophile, 2-mercaptoethanol. The influence of the variation of the substituents on the phenyl rings on the rate of reaction was quantified using the Hammett substituent constants and descriptors derived from ab initio or semiempirical calculations (atomic charges, HOMO, and LUMO). Statistically significant linear correlations between second-order rate constants and Hammett substituent constants, as well as energies of LUMO orbitals, were obtained. Substituents on both aroyl and arylamido moieties were shown to influence the reactivity of studied compounds toward thiols. The regioselectivity of reaction was confirmed by NMR spectroscopy. Exclusively beta-addition product with respect to the aroyl keto group was obtained. The determined enthalpy and entropy of activation were found to be in agreement with the proposed reaction mechanism, which includes a highly ordered transition state.",
publisher = "Springer Wien, Wien",
journal = "Monatshefte Fur Chemie",
title = "Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid arylamides toward 2-mercaptoethanol. A LFER study",
volume = "144",
number = "12",
pages = "1815-1824",
doi = "10.1007/s00706-013-1084-6"
}

Cvijetić, I., Vitorović-Todorović, M. D., Juranić, I. O.,& Drakulić, B. J.. (2013). Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid arylamides toward 2-mercaptoethanol. A LFER study. in Monatshefte Fur Chemie
Springer Wien, Wien., 144(12), 1815-1824.
https://doi.org/10.1007/s00706-013-1084-6

Cvijetić I, Vitorović-Todorović MD, Juranić IO, Drakulić BJ. Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid arylamides toward 2-mercaptoethanol. A LFER study. in Monatshefte Fur Chemie. 2013;144(12):1815-1824.
doi:10.1007/s00706-013-1084-6 .

Cvijetić, Ilija, Vitorović-Todorović, Maja D., Juranić, Ivan O., Drakulić, Branko J., "Reactivity of (E)-4-aryl-4-oxo-2-butenoic acid arylamides toward 2-mercaptoethanol. A LFER study" in Monatshefte Fur Chemie, 144, no. 12 (2013):1815-1824,
https://doi.org/10.1007/s00706-013-1084-6 . .

TY  - DATA
AU  - Grozdanović, Milica M.
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3476
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Supplementary data for article: Grozdanovic, M. M.; Drakulić, B. J.; Gavrović-Jankulović, M. Conformational Mobility of Active and E-64-Inhibited Actinidin. Biochimica et Biophysica Acta: General Subjects 2013, 1830 (10), 4790–4799. https://doi.org/10.1016/j.bbagen.2013.06.015
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3476
ER  - 

@misc{
author = "Grozdanović, Milica M. and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2013",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Supplementary data for article: Grozdanovic, M. M.; Drakulić, B. J.; Gavrović-Jankulović, M. Conformational Mobility of Active and E-64-Inhibited Actinidin. Biochimica et Biophysica Acta: General Subjects 2013, 1830 (10), 4790–4799. https://doi.org/10.1016/j.bbagen.2013.06.015",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3476"
}

Grozdanović, M. M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2013). Supplementary data for article: Grozdanovic, M. M.; Drakulić, B. J.; Gavrović-Jankulović, M. Conformational Mobility of Active and E-64-Inhibited Actinidin. Biochimica et Biophysica Acta: General Subjects 2013, 1830 (10), 4790–4799. https://doi.org/10.1016/j.bbagen.2013.06.015. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3476

Grozdanović MM, Drakulić BJ, Gavrović-Jankulović M. Supplementary data for article: Grozdanovic, M. M.; Drakulić, B. J.; Gavrović-Jankulović, M. Conformational Mobility of Active and E-64-Inhibited Actinidin. Biochimica et Biophysica Acta: General Subjects 2013, 1830 (10), 4790–4799. https://doi.org/10.1016/j.bbagen.2013.06.015. in Biochimica et Biophysica Acta: General Subjects. 2013;.
https://hdl.handle.net/21.15107/rcub_cherry_3476 .

Grozdanović, Milica M., Drakulić, Branko J., Gavrović-Jankulović, Marija, "Supplementary data for article: Grozdanovic, M. M.; Drakulić, B. J.; Gavrović-Jankulović, M. Conformational Mobility of Active and E-64-Inhibited Actinidin. Biochimica et Biophysica Acta: General Subjects 2013, 1830 (10), 4790–4799. https://doi.org/10.1016/j.bbagen.2013.06.015" in Biochimica et Biophysica Acta: General Subjects (2013),
https://hdl.handle.net/21.15107/rcub_cherry_3476 .

TY  - JOUR
AU  - Grozdanović, Milica M.
AU  - Drakulić, Branko J.
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1398
AB  - Background: Actinidin, a protease from kiwifruit, belongs to the C1 family of cysteine proteases. Cysteine proteases were found to be involved in many disease states and are valid therapeutic targets. Actinidin has a wide pH activity range and wide substrate specificity, which makes it a good model system for studying enzyme-substrate interactions. Methods: The influence of inhibitor (E-64) binding on the conformation of actinidin was examined by 2D PAGE, circular dichroism (CD) spectroscopy, hydrophobic ligand binding assay, and molecular dynamics simulations. Results: Significant differences were observed in electrophoretic mobility of proteolytically active and E-64-inhibited actinidin. CD spectrometry and hydrophobic ligand binding assay revealed a difference in conformation between active and inhibited actinidin. Molecular dynamics simulations showed that a loop defined by amino-acid residues 88-104 had greater conformational mobility in the inhibited enzyme than in the active one. During MD simulations, the covalently bound inhibitor was found to change its conformation from extended to folded, with the guanidino moiety approaching the carboxylate. Conclusions: Conformational mobility of actinidin changes upon binding of the inhibitor, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme. Drastic conformational mobility of E-64, a common inhibitor of cysteine proteases found in many crystal structures stored in PDB, was also observed. General significance: The analysis of structural changes which occur upon binding of an inhibitor to a cysteine protease provides a valuable starting point for the future design of therapeutic agents.
PB  - Elsevier Science Bv, Amsterdam
T2  - Biochimica et Biophysica Acta: General Subjects
T1  - Conformational mobility of active and E-64-inhibited actinidin
VL  - 1830
IS  - 10
SP  - 4790
EP  - 4799
DO  - 10.1016/j.bbagen.2013.06.015
ER  - 

@article{
author = "Grozdanović, Milica M. and Drakulić, Branko J. and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Background: Actinidin, a protease from kiwifruit, belongs to the C1 family of cysteine proteases. Cysteine proteases were found to be involved in many disease states and are valid therapeutic targets. Actinidin has a wide pH activity range and wide substrate specificity, which makes it a good model system for studying enzyme-substrate interactions. Methods: The influence of inhibitor (E-64) binding on the conformation of actinidin was examined by 2D PAGE, circular dichroism (CD) spectroscopy, hydrophobic ligand binding assay, and molecular dynamics simulations. Results: Significant differences were observed in electrophoretic mobility of proteolytically active and E-64-inhibited actinidin. CD spectrometry and hydrophobic ligand binding assay revealed a difference in conformation between active and inhibited actinidin. Molecular dynamics simulations showed that a loop defined by amino-acid residues 88-104 had greater conformational mobility in the inhibited enzyme than in the active one. During MD simulations, the covalently bound inhibitor was found to change its conformation from extended to folded, with the guanidino moiety approaching the carboxylate. Conclusions: Conformational mobility of actinidin changes upon binding of the inhibitor, leading to a sequence of events that enables water and ions to protrude into a newly formed cavity of the inhibited enzyme. Drastic conformational mobility of E-64, a common inhibitor of cysteine proteases found in many crystal structures stored in PDB, was also observed. General significance: The analysis of structural changes which occur upon binding of an inhibitor to a cysteine protease provides a valuable starting point for the future design of therapeutic agents.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Biochimica et Biophysica Acta: General Subjects",
title = "Conformational mobility of active and E-64-inhibited actinidin",
volume = "1830",
number = "10",
pages = "4790-4799",
doi = "10.1016/j.bbagen.2013.06.015"
}

Grozdanović, M. M., Drakulić, B. J.,& Gavrović-Jankulović, M.. (2013). Conformational mobility of active and E-64-inhibited actinidin. in Biochimica et Biophysica Acta: General Subjects
Elsevier Science Bv, Amsterdam., 1830(10), 4790-4799.
https://doi.org/10.1016/j.bbagen.2013.06.015

Grozdanović MM, Drakulić BJ, Gavrović-Jankulović M. Conformational mobility of active and E-64-inhibited actinidin. in Biochimica et Biophysica Acta: General Subjects. 2013;1830(10):4790-4799.
doi:10.1016/j.bbagen.2013.06.015 .

Grozdanović, Milica M., Drakulić, Branko J., Gavrović-Jankulović, Marija, "Conformational mobility of active and E-64-inhibited actinidin" in Biochimica et Biophysica Acta: General Subjects, 1830, no. 10 (2013):4790-4799,
https://doi.org/10.1016/j.bbagen.2013.06.015 . .

TY  - JOUR
AU  - Sovilj, Sofija P.
AU  - Mitić, Dragana
AU  - Drakulić, Branko J.
AU  - Milenković, Marina
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1247
AB  - Five new dioxomolybdenum(VI) complexes of the general formula [MoO2(Rdtc)(2)], 1-5, where Rdtc(-) refer to piperidine (Pipdtc), 4-morpholine (Morphdtc), 4-thiomorpholine (Timdtc), piperazine (Pzdtc) or N-methylpiperazine (N-Mepzdtc) dithiocarbamates, respectively, have been prepared. The complexes were characterized by elemental analysis, conductometric measurements, electronic, IR and NMR spectroscopy. The complexes 1-5 contain a cis-MoO2 group and have an octahedral geometry. Two dithiocarbamato ions join as bidentates with both the sulfur atoms to the molybdenum atom. The presence of different heteroatoms in the piperidino moiety influences the v(C=N) and v(C=S) vibrations, which wavelengths decrease in the order: Pipdtc  gt  N-Mepzdtc  gt  Morphdtc  gt  Pzdtc  gt  Timdtc ligands. Based on their spectral data, the molecular structures of complexes 1-5 were optimized at the semi-empirical molecular-orbital level, and the geometries, as obtained from calculations, are described. The antimicrobial activities of the complexes were tested against nine different laboratory control strains of bacteria and two strains of the yeast Candida albicans. All the tested strains were sensitive. Complexes bearing heteroatom in position 4 of piperidine moiety were significantly more potent against the tested bacteria compared to the corresponding ligands.
AB  - Sintetisano je pet novih dioksomolibden(VI) kompleksa, opšte formule [MoO2(Rdtc-)2], sa Rdtc- ligandima: piperidin- (Pipdtc), 4-morfolin- (Morphdtc), 4-tiomorfolin- (Timdtc), piperazin- (Pzdtc) i N-metilpiperazin- (N-Mepzdtc) ditiokarbamatima. Kompleksi su okarakterisani elementalnom analizom, IR i NMR spektroskopijom kao i merenjem molarne provodljivosti. Pretpostavljena geometrija svih kompleksa je oktaedarska. Rdtc- ligandi su bidentatno koordinovani preko oba atoma sumpora za atom molibdena. Prisustvo različitih heteroatoma utiče na promenu položaja v(C=N) i v(C=S) vibracija, čiji opada sledećim redom liganada: Pipdtc  gt  N-Mepzdtc  gt  Morphdt  gt  Pzdtc  gt  Timdtc. Na osnovu spektralnih podataka, strukture svih kompleksa su optimizovane na semiempirijskom molekulsko-orbitalnom nivou upotrebom PM6 metoda. Antimikrobna aktivnost ispitivana je na jedanaest različitih patogena. Uočeno je da kompleksi koji imaju heteroatom u položaju 4 piperidinskog prstena ispoljavaju značajno veću jačinu antimikrobnog dejstva prema bakterijama, u poređenju sa odgovarajućim ligandima.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Spectroscopic properties and antimicrobial activity of dioxomolybdenum(VI) complexes with heterocyclic S,S '-ligands
T1  - Spektroskopska svojstva i antimikrobna aktivnost dioksomolibden(VI) kompleksa sa heterocikličnim S,S'-ligandima
VL  - 77
IS  - 1
SP  - 53
EP  - 66
DO  - 10.2298/JSC110328160S
ER  - 

@article{
author = "Sovilj, Sofija P. and Mitić, Dragana and Drakulić, Branko J. and Milenković, Marina",
year = "2012",
abstract = "Five new dioxomolybdenum(VI) complexes of the general formula [MoO2(Rdtc)(2)], 1-5, where Rdtc(-) refer to piperidine (Pipdtc), 4-morpholine (Morphdtc), 4-thiomorpholine (Timdtc), piperazine (Pzdtc) or N-methylpiperazine (N-Mepzdtc) dithiocarbamates, respectively, have been prepared. The complexes were characterized by elemental analysis, conductometric measurements, electronic, IR and NMR spectroscopy. The complexes 1-5 contain a cis-MoO2 group and have an octahedral geometry. Two dithiocarbamato ions join as bidentates with both the sulfur atoms to the molybdenum atom. The presence of different heteroatoms in the piperidino moiety influences the v(C=N) and v(C=S) vibrations, which wavelengths decrease in the order: Pipdtc  gt  N-Mepzdtc  gt  Morphdtc  gt  Pzdtc  gt  Timdtc ligands. Based on their spectral data, the molecular structures of complexes 1-5 were optimized at the semi-empirical molecular-orbital level, and the geometries, as obtained from calculations, are described. The antimicrobial activities of the complexes were tested against nine different laboratory control strains of bacteria and two strains of the yeast Candida albicans. All the tested strains were sensitive. Complexes bearing heteroatom in position 4 of piperidine moiety were significantly more potent against the tested bacteria compared to the corresponding ligands., Sintetisano je pet novih dioksomolibden(VI) kompleksa, opšte formule [MoO2(Rdtc-)2], sa Rdtc- ligandima: piperidin- (Pipdtc), 4-morfolin- (Morphdtc), 4-tiomorfolin- (Timdtc), piperazin- (Pzdtc) i N-metilpiperazin- (N-Mepzdtc) ditiokarbamatima. Kompleksi su okarakterisani elementalnom analizom, IR i NMR spektroskopijom kao i merenjem molarne provodljivosti. Pretpostavljena geometrija svih kompleksa je oktaedarska. Rdtc- ligandi su bidentatno koordinovani preko oba atoma sumpora za atom molibdena. Prisustvo različitih heteroatoma utiče na promenu položaja v(C=N) i v(C=S) vibracija, čiji opada sledećim redom liganada: Pipdtc  gt  N-Mepzdtc  gt  Morphdt  gt  Pzdtc  gt  Timdtc. Na osnovu spektralnih podataka, strukture svih kompleksa su optimizovane na semiempirijskom molekulsko-orbitalnom nivou upotrebom PM6 metoda. Antimikrobna aktivnost ispitivana je na jedanaest različitih patogena. Uočeno je da kompleksi koji imaju heteroatom u položaju 4 piperidinskog prstena ispoljavaju značajno veću jačinu antimikrobnog dejstva prema bakterijama, u poređenju sa odgovarajućim ligandima.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Spectroscopic properties and antimicrobial activity of dioxomolybdenum(VI) complexes with heterocyclic S,S '-ligands, Spektroskopska svojstva i antimikrobna aktivnost dioksomolibden(VI) kompleksa sa heterocikličnim S,S'-ligandima",
volume = "77",
number = "1",
pages = "53-66",
doi = "10.2298/JSC110328160S"
}

Sovilj, S. P., Mitić, D., Drakulić, B. J.,& Milenković, M.. (2012). Spectroscopic properties and antimicrobial activity of dioxomolybdenum(VI) complexes with heterocyclic S,S '-ligands. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 77(1), 53-66.
https://doi.org/10.2298/JSC110328160S

Sovilj SP, Mitić D, Drakulić BJ, Milenković M. Spectroscopic properties and antimicrobial activity of dioxomolybdenum(VI) complexes with heterocyclic S,S '-ligands. in Journal of the Serbian Chemical Society. 2012;77(1):53-66.
doi:10.2298/JSC110328160S .

Sovilj, Sofija P., Mitić, Dragana, Drakulić, Branko J., Milenković, Marina, "Spectroscopic properties and antimicrobial activity of dioxomolybdenum(VI) complexes with heterocyclic S,S '-ligands" in Journal of the Serbian Chemical Society, 77, no. 1 (2012):53-66,
https://doi.org/10.2298/JSC110328160S . .

TY  - JOUR
AU  - Vitorović-Todorović, Maja D.
AU  - Cvijetić, Ilija
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1574
AB  - The 3D-QSAR analysis based on alignment independent descriptors (GRIND-2) was performed on the set of 110 structurally diverse, dual binding AChE reversible inhibitors. Three separate models were built, based on different conformations, generated following next criteria: (i) minimum energy conformations, (ii) conformation most similar to the co-crystalized ligand conformation, and (iii) docked conformation. We found that regardless on conformation used, all the three models had good statistic and predictivity. The models revealed the importance of protonated pyridine nitrogen of tacrine moiety for anti AChE activity, and recognized HBA and HBD interactions as highly important for the potency. This was revealed by the variables associated with protonated pyridinium nitrogen, and the two amino groups of the linker. MIFs calculated with the N1= (pyridinium nitrogen) and the DRY GRID probes in the AChE active site enabled us to establish the relationship between amino acid residues within AChE active site and the variables having high impact on models. External predictive power of the models was tested on the set of 40 AChE reversible inhibitors, most of them structurally different from the training set. Some of those compounds were tested on the different enzyme source. We found that external predictivity was highly sensitive on conformations used. Model based on docked conformations had superior predictive ability, emphasizing the need for the employment of conformations built by taking into account geometrical restrictions of AChE active site gorge. (C) 2012 Elsevier Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Journal of Molecular Graphics and Modelling
T1  - The 3D-QSAR study of 110 diverse, dual binding, acetylcholinesterase inhibitors based on alignment independent descriptors (GRIND-2). The effects of conformation on predictive power and interpretability of the models
VL  - 38
SP  - 194
EP  - 210
DO  - 10.1016/j.jmgm.2012.08.001
ER  - 

@article{
author = "Vitorović-Todorović, Maja D. and Cvijetić, Ilija and Juranić, Ivan O. and Drakulić, Branko J.",
year = "2012",
abstract = "The 3D-QSAR analysis based on alignment independent descriptors (GRIND-2) was performed on the set of 110 structurally diverse, dual binding AChE reversible inhibitors. Three separate models were built, based on different conformations, generated following next criteria: (i) minimum energy conformations, (ii) conformation most similar to the co-crystalized ligand conformation, and (iii) docked conformation. We found that regardless on conformation used, all the three models had good statistic and predictivity. The models revealed the importance of protonated pyridine nitrogen of tacrine moiety for anti AChE activity, and recognized HBA and HBD interactions as highly important for the potency. This was revealed by the variables associated with protonated pyridinium nitrogen, and the two amino groups of the linker. MIFs calculated with the N1= (pyridinium nitrogen) and the DRY GRID probes in the AChE active site enabled us to establish the relationship between amino acid residues within AChE active site and the variables having high impact on models. External predictive power of the models was tested on the set of 40 AChE reversible inhibitors, most of them structurally different from the training set. Some of those compounds were tested on the different enzyme source. We found that external predictivity was highly sensitive on conformations used. Model based on docked conformations had superior predictive ability, emphasizing the need for the employment of conformations built by taking into account geometrical restrictions of AChE active site gorge. (C) 2012 Elsevier Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Journal of Molecular Graphics and Modelling",
title = "The 3D-QSAR study of 110 diverse, dual binding, acetylcholinesterase inhibitors based on alignment independent descriptors (GRIND-2). The effects of conformation on predictive power and interpretability of the models",
volume = "38",
pages = "194-210",
doi = "10.1016/j.jmgm.2012.08.001"
}

Vitorović-Todorović, M. D., Cvijetić, I., Juranić, I. O.,& Drakulić, B. J.. (2012). The 3D-QSAR study of 110 diverse, dual binding, acetylcholinesterase inhibitors based on alignment independent descriptors (GRIND-2). The effects of conformation on predictive power and interpretability of the models. in Journal of Molecular Graphics and Modelling
Elsevier Science Inc, New York., 38, 194-210.
https://doi.org/10.1016/j.jmgm.2012.08.001

Vitorović-Todorović MD, Cvijetić I, Juranić IO, Drakulić BJ. The 3D-QSAR study of 110 diverse, dual binding, acetylcholinesterase inhibitors based on alignment independent descriptors (GRIND-2). The effects of conformation on predictive power and interpretability of the models. in Journal of Molecular Graphics and Modelling. 2012;38:194-210.
doi:10.1016/j.jmgm.2012.08.001 .

Vitorović-Todorović, Maja D., Cvijetić, Ilija, Juranić, Ivan O., Drakulić, Branko J., "The 3D-QSAR study of 110 diverse, dual binding, acetylcholinesterase inhibitors based on alignment independent descriptors (GRIND-2). The effects of conformation on predictive power and interpretability of the models" in Journal of Molecular Graphics and Modelling, 38 (2012):194-210,
https://doi.org/10.1016/j.jmgm.2012.08.001 . .

TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Žižak, Željko S.
AU  - Stanojković, Tatjana
AU  - Juranić, Zorica D.
AU  - Terzić-Jovanović, Nataša
AU  - Opsenica, Igor
AU  - Opsenica, Dejan M.
AU  - Juranić, Ivan O.
AU  - Drakulić, Branko J.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1120
AB  - An alignment-free 3D QSAR study on antiproliferative activity of the thirty-three 1,2,4,5-tetraoxane derivatives toward two human dedifferentiated cell lines was reported. GRIND methodology, where descriptors are derived from GRID molecular interaction fields (MIF), were used It was found that pharmacophoric pattern attributed to the most potent derivatives Include amido NH of the primary or secondary amide, and the acetoxy fragments at positions 7 and 12 of steroid core which are, along with the tetraoxane ring, common for all studied compounds. Independently, simple multiple regression model obtained by using the whole-molecular properties, confirmed that the hydrophobicity and the H-bond donor properties are the main parameters influencing potency of compounds toward human cervix carcinoma (HeLa) and human malignant melanoma (FemX) cell lines Corollary, similar structural motifs are found to be Important for the potency toward both examined cell lines. (C) 2010 Elsevier Masson SAS. All rights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - An alignment independent 3D QSAR study of the antiproliferative activity of 1,2,4,5-tetraoxanes
VL  - 45
IS  - 10
SP  - 4570
EP  - 4577
DO  - 10.1016/j.ejmech.2010.07.019
ER  - 

@article{
author = "Cvijetić, Ilija and Žižak, Željko S. and Stanojković, Tatjana and Juranić, Zorica D. and Terzić-Jovanović, Nataša and Opsenica, Igor and Opsenica, Dejan M. and Juranić, Ivan O. and Drakulić, Branko J.",
year = "2010",
abstract = "An alignment-free 3D QSAR study on antiproliferative activity of the thirty-three 1,2,4,5-tetraoxane derivatives toward two human dedifferentiated cell lines was reported. GRIND methodology, where descriptors are derived from GRID molecular interaction fields (MIF), were used It was found that pharmacophoric pattern attributed to the most potent derivatives Include amido NH of the primary or secondary amide, and the acetoxy fragments at positions 7 and 12 of steroid core which are, along with the tetraoxane ring, common for all studied compounds. Independently, simple multiple regression model obtained by using the whole-molecular properties, confirmed that the hydrophobicity and the H-bond donor properties are the main parameters influencing potency of compounds toward human cervix carcinoma (HeLa) and human malignant melanoma (FemX) cell lines Corollary, similar structural motifs are found to be Important for the potency toward both examined cell lines. (C) 2010 Elsevier Masson SAS. All rights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "An alignment independent 3D QSAR study of the antiproliferative activity of 1,2,4,5-tetraoxanes",
volume = "45",
number = "10",
pages = "4570-4577",
doi = "10.1016/j.ejmech.2010.07.019"
}

Cvijetić, I., Žižak, Ž. S., Stanojković, T., Juranić, Z. D., Terzić-Jovanović, N., Opsenica, I., Opsenica, D. M., Juranić, I. O.,& Drakulić, B. J.. (2010). An alignment independent 3D QSAR study of the antiproliferative activity of 1,2,4,5-tetraoxanes. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 45(10), 4570-4577.
https://doi.org/10.1016/j.ejmech.2010.07.019

Cvijetić I, Žižak ŽS, Stanojković T, Juranić ZD, Terzić-Jovanović N, Opsenica I, Opsenica DM, Juranić IO, Drakulić BJ. An alignment independent 3D QSAR study of the antiproliferative activity of 1,2,4,5-tetraoxanes. in European Journal of Medicinal Chemistry. 2010;45(10):4570-4577.
doi:10.1016/j.ejmech.2010.07.019 .

Cvijetić, Ilija, Žižak, Željko S., Stanojković, Tatjana, Juranić, Zorica D., Terzić-Jovanović, Nataša, Opsenica, Igor, Opsenica, Dejan M., Juranić, Ivan O., Drakulić, Branko J., "An alignment independent 3D QSAR study of the antiproliferative activity of 1,2,4,5-tetraoxanes" in European Journal of Medicinal Chemistry, 45, no. 10 (2010):4570-4577,
https://doi.org/10.1016/j.ejmech.2010.07.019 . .

TY  - JOUR
AU  - Pastor, Ferenc
AU  - Drakulić, Branko J.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1050
AB  - Half-wave reduction potentials of a set of twelve (E)-4-aryl-4-oxo-2-butenoic acids obtained by direct current polarography in methanol are reported. E(1/2) is correlated with Hammett sigma values as well as with values of frontier molecular orbitals calculated at a semiempirical molecular orbital level. Constant potential electrolysis of a representative compound shows that the first polarographic wave corresponds to one-electron reduction. The isolation of the product proves reduction of the activated double bond. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Tetrahedron Letters
T1  - Linear free energy relationships of half-wave reduction potentials of (E)-4-aryl-4-oxo-2-butenoic acids
VL  - 51
IS  - 4
SP  - 734
EP  - 738
DO  - 10.1016/j.tetlet.2009.11.129
ER  - 

@article{
author = "Pastor, Ferenc and Drakulić, Branko J.",
year = "2010",
abstract = "Half-wave reduction potentials of a set of twelve (E)-4-aryl-4-oxo-2-butenoic acids obtained by direct current polarography in methanol are reported. E(1/2) is correlated with Hammett sigma values as well as with values of frontier molecular orbitals calculated at a semiempirical molecular orbital level. Constant potential electrolysis of a representative compound shows that the first polarographic wave corresponds to one-electron reduction. The isolation of the product proves reduction of the activated double bond. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Tetrahedron Letters",
title = "Linear free energy relationships of half-wave reduction potentials of (E)-4-aryl-4-oxo-2-butenoic acids",
volume = "51",
number = "4",
pages = "734-738",
doi = "10.1016/j.tetlet.2009.11.129"
}

Pastor, F.,& Drakulić, B. J.. (2010). Linear free energy relationships of half-wave reduction potentials of (E)-4-aryl-4-oxo-2-butenoic acids. in Tetrahedron Letters
Pergamon-Elsevier Science Ltd, Oxford., 51(4), 734-738.
https://doi.org/10.1016/j.tetlet.2009.11.129

Pastor F, Drakulić BJ. Linear free energy relationships of half-wave reduction potentials of (E)-4-aryl-4-oxo-2-butenoic acids. in Tetrahedron Letters. 2010;51(4):734-738.
doi:10.1016/j.tetlet.2009.11.129 .

Pastor, Ferenc, Drakulić, Branko J., "Linear free energy relationships of half-wave reduction potentials of (E)-4-aryl-4-oxo-2-butenoic acids" in Tetrahedron Letters, 51, no. 4 (2010):734-738,
https://doi.org/10.1016/j.tetlet.2009.11.129 . .