TY  - JOUR
AU  - Cvijetić, Ilija
AU  - Petrović, D.D.
AU  - Verbić, Tatjana
AU  - Juranić, Ivan
AU  - Drakulić, Branko
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2669
AB  - Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) × 104 M-1 at 37 ± 1 °C), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) × 104 M-1 at 37 ± 1 °C). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster's non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA) was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex. © 2014 by the authors.
T2  - ADMET and DMPK
T1  - Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters
VL  - 2
IS  - 2
SP  - 126
EP  - 142
DO  - 10.5599/admet.2.2.28
ER  - 

@article{
author = "Cvijetić, Ilija and Petrović, D.D. and Verbić, Tatjana and Juranić, Ivan and Drakulić, Branko",
year = "2014",
abstract = "Interactions of 2-[(carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic acid (compound 1) and its mono-Me ester (compound 2) with the human serum albumin (HSA) have been studied by fluorescence spectroscopy. Comp. 1 exerts antiproliferative activity toward human tumor cells and significant selectivity (tumor vs. healthy cells) in vitro. Competitive binding study with warfarin and ibuprofen as binding site probes, revealed that one molecule of comp. 1 selectively binds to HSA Sudlow site I (warfarin site) with moderate binding constant (Kb = (2.8 ± 0.5) × 104 M-1 at 37 ± 1 °C), while comp. 2 binds to Sudlow site II (Kb = (3.2 ± 0.9) × 104 M-1 at 37 ± 1 °C). Fluorescence quenching at different temperatures was analyzed using classical Stern-Volmer equation, and a static quenching mechanism was proposed. Energy resonance transfer between HSA and comp. 1 was examined according to Förster's non-radiative energy transfer theory. Distance of about 10 Å between ligand and Trp214 (HSA) was obtained. Docking studies confirmed HSA Sudlow site I as a preferable comp. 1 binding site, and Sudlow site II as comp. 2 binding site. Molecular dynamics simulations proved the stability of comp. 1/HSA complex. © 2014 by the authors.",
journal = "ADMET and DMPK",
title = "Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters",
volume = "2",
number = "2",
pages = "126-142",
doi = "10.5599/admet.2.2.28"
}

Cvijetić, I., Petrović, D.D., Verbić, T., Juranić, I.,& Drakulić, B.. (2014). Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters. in ADMET and DMPK, 2(2), 126-142.
https://doi.org/10.5599/admet.2.2.28

Cvijetić I, Petrović D, Verbić T, Juranić I, Drakulić B. Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters. in ADMET and DMPK. 2014;2(2):126-142.
doi:10.5599/admet.2.2.28 .

Cvijetić, Ilija, Petrović, D.D., Verbić, Tatjana, Juranić, Ivan, Drakulić, Branko, "Human Serum Albumin Binding of 2-[(Carboxymethyl)sulfanyl]-4-oxo-4-(4-tert-butylphenyl)butanoic Acid and its Mono-Me Esters" in ADMET and DMPK, 2, no. 2 (2014):126-142,
https://doi.org/10.5599/admet.2.2.28 . .

TY  - JOUR
AU  - Perovic, I.
AU  - Milovanovic, M.
AU  - Stanić, Dragana
AU  - Burazer, Lidija M.
AU  - Petrović, D.
AU  - Milčić-Matić, Natalija
AU  - Gafvelin, Guro
AU  - van Hage, Marianne
AU  - Jankov, Ratko M.
AU  - Ćirković-Veličković, Tanja
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4324
AB  - Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.
PB  - Wiley-Blackwell Publishing, Inc, Malden
T2  - Clinical and Experimental Allergy
T1  - Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation
VL  - 39
IS  - 3
SP  - 435
EP  - 446
DO  - 10.1111/j.1365-2222.2008.03158.x
ER  - 

@article{
author = "Perovic, I. and Milovanovic, M. and Stanić, Dragana and Burazer, Lidija M. and Petrović, D. and Milčić-Matić, Natalija and Gafvelin, Guro and van Hage, Marianne and Jankov, Ratko M. and Ćirković-Veličković, Tanja",
year = "2009",
abstract = "Treating allergies with modified allergens is an approach to make the treatment safer and more efficient. Art v 1 is the most prominent allergen of mugwort pollen and a significant cause of hayfever around Europe. The aim of this study was to reduce the allergenicity of Art v 1 by acetylation, and to investigate the capacity of the modified protein to generate blocking antibodies. The reduction of allergenicity of Art v 1 following acetylation was monitored by immunoblot, ELISA inhibition using a pool of sera from mugwort pollen allergic patients, basophil activation assay and by skin prick testing of mugwort-allergic patients. Rabbits were immunized against Art v 1 and acetylated Art v 1 (acArt v 1) and the rabbit antisera were tested for their capacity to block human IgE binding in ELISA. Human T cell proliferation against Art v 1 and acArt v 1 was examined in peripheral blood mononuclear cells (PBMCs) of mugwort pollen allergic patients and cytokine release in PBMC cultures was monitored. Acetylation of Art v 1 gave a derivative of reduced allergenicity in the in vitro and ex vivo tests applied. The skin test reactivity to acArt v 1 was significantly reduced in 19 patients when compared with the reactivity to Art v 1. Rabbit antibodies to acArt v 1 and Art v 1 showed similar capacity to block human IgE binding to Art v 1 in inhibition ELISA. Both proteins were able to induce proliferation of PBMCs and CD3/CD4(+) cells of mugwort-allergic patients. Release of IL-5 was significantly reduced in cultures stimulated with acArt v 1. Art v 1 modified by acetylation had a significantly reduced allergenicity in vitro and in vivo, while its immunogenicity was retained. Modification of allergens by acetylation could be a new strategy for allergen-specific immunotherapy. Cite this as: I. Perovic, M. Milovanovic, D. Stanic, L. Burazer, D. Petrovic, N. Milcic-Matic, G. Gafvelin, M. van Hage, R. Jankov and T. Cirkovic Velickovic, Clinical and Experimental Allergy, 2009 (39) 435-446.",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Clinical and Experimental Allergy",
title = "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation",
volume = "39",
number = "3",
pages = "435-446",
doi = "10.1111/j.1365-2222.2008.03158.x"
}

Perovic, I., Milovanovic, M., Stanić, D., Burazer, L. M., Petrović, D., Milčić-Matić, N., Gafvelin, G., van Hage, M., Jankov, R. M.,& Ćirković-Veličković, T.. (2009). Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy
Wiley-Blackwell Publishing, Inc, Malden., 39(3), 435-446.
https://doi.org/10.1111/j.1365-2222.2008.03158.x

Perovic I, Milovanovic M, Stanić D, Burazer LM, Petrović D, Milčić-Matić N, Gafvelin G, van Hage M, Jankov RM, Ćirković-Veličković T. Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation. in Clinical and Experimental Allergy. 2009;39(3):435-446.
doi:10.1111/j.1365-2222.2008.03158.x .

Perovic, I., Milovanovic, M., Stanić, Dragana, Burazer, Lidija M., Petrović, D., Milčić-Matić, Natalija, Gafvelin, Guro, van Hage, Marianne, Jankov, Ratko M., Ćirković-Veličković, Tanja, "Allergenicity and immunogenicity of the major mugwort pollen allergen Art v 1 chemically modified by acetylation" in Clinical and Experimental Allergy, 39, no. 3 (2009):435-446,
https://doi.org/10.1111/j.1365-2222.2008.03158.x . .

TY  - JOUR
AU  - Petrović, S D
AU  - Gorunović, M S
AU  - Vajs, Vlatka
AU  - Dermanovic, M
PY  - 1996
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2795
PB  - Govi-Verlag Pharmazeutischer Verlag GmbH
T2  - Pharmazie
T1  - Triterpenoids from Hieracium plumulosum A. Kerner, L., Asteraceae
VL  - 51
IS  - 12
SP  - 996
EP  - 997
UR  - https://hdl.handle.net/21.15107/rcub_cer_2795
ER  - 

@article{
author = "Petrović, S D and Gorunović, M S and Vajs, Vlatka and Dermanovic, M",
year = "1996",
publisher = "Govi-Verlag Pharmazeutischer Verlag GmbH",
journal = "Pharmazie",
title = "Triterpenoids from Hieracium plumulosum A. Kerner, L., Asteraceae",
volume = "51",
number = "12",
pages = "996-997",
url = "https://hdl.handle.net/21.15107/rcub_cer_2795"
}

Petrović, S. D., Gorunović, M. S., Vajs, V.,& Dermanovic, M.. (1996). Triterpenoids from Hieracium plumulosum A. Kerner, L., Asteraceae. in Pharmazie
Govi-Verlag Pharmazeutischer Verlag GmbH., 51(12), 996-997.
https://hdl.handle.net/21.15107/rcub_cer_2795

Petrović SD, Gorunović MS, Vajs V, Dermanovic M. Triterpenoids from Hieracium plumulosum A. Kerner, L., Asteraceae. in Pharmazie. 1996;51(12):996-997.
https://hdl.handle.net/21.15107/rcub_cer_2795 .

Petrović, S D, Gorunović, M S, Vajs, Vlatka, Dermanovic, M, "Triterpenoids from Hieracium plumulosum A. Kerner, L., Asteraceae" in Pharmazie, 51, no. 12 (1996):996-997,
https://hdl.handle.net/21.15107/rcub_cer_2795 .

TY  - JOUR
AU  - Antonović, D G
AU  - Vajs, Vlatka
AU  - Stojanović, N D
AU  - Nikolić, A D
AU  - Petrović, S D
PY  - 1992
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2790
AB  - As a part of a study on the structural characteristics of some new various N-alkyl-N-substituted 2-phenylacetamides the infrared and 1 H N.M.R. spectra were obtained and interpreted. The synthesis of a various N-n-propyl-N-alkyl 2-phenylacetamides of the general formula PhCH 2 CON(nPr)R, wherein R is ethyl, isopropyl, n-butyl, t-butyl and cyclohexyl, were performed. The corresponding mixed secondary amines of the type HNnPrR were obtained by catalytic hydrogenation of the synthetized propylidenealkylamines. The 1 H N.M.R. spectra of these unsymmetrically N,N-disubstituted amides have been studied and the peaks have been assigned in each cases to two possible conformational isomers, arising from the lack of free rotation about the C(O)N bond. These results are in accordance with our previous investigation of the structure of N-substituted 2-phenylacetamides. © 1992.
PB  - Elsevier Science Publishers B.V
T2  - Journal of Molecular Structure
T1  - Conformations in unsymmetrically N-n-propyl-N-substituted 2-phenylacetamides
VL  - 266
IS  - C
SP  - 255
EP  - 258
DO  - 10.1016/0022-2860(92)80075-S
ER  - 

@article{
author = "Antonović, D G and Vajs, Vlatka and Stojanović, N D and Nikolić, A D and Petrović, S D",
year = "1992",
abstract = "As a part of a study on the structural characteristics of some new various N-alkyl-N-substituted 2-phenylacetamides the infrared and 1 H N.M.R. spectra were obtained and interpreted. The synthesis of a various N-n-propyl-N-alkyl 2-phenylacetamides of the general formula PhCH 2 CON(nPr)R, wherein R is ethyl, isopropyl, n-butyl, t-butyl and cyclohexyl, were performed. The corresponding mixed secondary amines of the type HNnPrR were obtained by catalytic hydrogenation of the synthetized propylidenealkylamines. The 1 H N.M.R. spectra of these unsymmetrically N,N-disubstituted amides have been studied and the peaks have been assigned in each cases to two possible conformational isomers, arising from the lack of free rotation about the C(O)N bond. These results are in accordance with our previous investigation of the structure of N-substituted 2-phenylacetamides. © 1992.",
publisher = "Elsevier Science Publishers B.V",
journal = "Journal of Molecular Structure",
title = "Conformations in unsymmetrically N-n-propyl-N-substituted 2-phenylacetamides",
volume = "266",
number = "C",
pages = "255-258",
doi = "10.1016/0022-2860(92)80075-S"
}

Antonović, D. G., Vajs, V., Stojanović, N. D., Nikolić, A. D.,& Petrović, S. D.. (1992). Conformations in unsymmetrically N-n-propyl-N-substituted 2-phenylacetamides. in Journal of Molecular Structure
Elsevier Science Publishers B.V., 266(C), 255-258.
https://doi.org/10.1016/0022-2860(92)80075-S

Antonović DG, Vajs V, Stojanović ND, Nikolić AD, Petrović SD. Conformations in unsymmetrically N-n-propyl-N-substituted 2-phenylacetamides. in Journal of Molecular Structure. 1992;266(C):255-258.
doi:10.1016/0022-2860(92)80075-S .

Antonović, D G, Vajs, Vlatka, Stojanović, N D, Nikolić, A D, Petrović, S D, "Conformations in unsymmetrically N-n-propyl-N-substituted 2-phenylacetamides" in Journal of Molecular Structure, 266, no. C (1992):255-258,
https://doi.org/10.1016/0022-2860(92)80075-S . .