TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3432
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of itsreactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of itsreactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "108787",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311, 108787.
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:108787.
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):108787,
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3053
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its
reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its
reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "108787",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311, 108787.
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:108787.
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):108787,
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - JOUR
AU  - Vitorović-Todorović, Maja D.
AU  - Koukoulitsa, Catherine
AU  - Juranić, Ivan
AU  - Mandić, Ljuba M.
AU  - Drakulić, Branko
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2688
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 and Mandić, Ljuba M. and Drakulić, Branko",
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., Mandić, L. M.,& Drakulić, B.. (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 I, Mandić LM, Drakulić B. 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, Mandić, Ljuba M., Drakulić, Branko, "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  - Vitorović-Todorović, Maja D.
AU  - Koukoulitsa, Catherine
AU  - Juranić, Ivan
AU  - Mandić, Ljuba M.
AU  - Drakulić, Branko
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3134
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 and Mandić, Ljuba M. and Drakulić, Branko",
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., Mandić, L. M.,& Drakulić, B.. (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 I, Mandić LM, Drakulić B. 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, Mandić, Ljuba M., Drakulić, Branko, "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  - Aćimović, Jelena M.
AU  - Stanimirovic, Bojana D.
AU  - Todorović, Nina
AU  - Jovanović, Vesna B.
AU  - Mandić, Ljuba M.
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/719
AB  - Methylglyoxal (MG), a reactive alpha-oxoaldehyde that is produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation, reacts with the thiol groups (in addition to the amino and guanidino groups) of proteins. This causes protein modification, formation of advanced glycated end products (AGEs) and cross-linking. Low molecular mass thiols can be used as competitive targets for MG, preventing the reactions mentioned above. Therefore, this paper investigated how the microenvironment of the thiol group in low molecular mass thiols (cysteine, N-acetylcysteine (NAcCys), carboxymethylcysteine (CMC) and glutathione (GSH)) and human serum albumin (HSA) affected the thiol reaction with MG. The SH group reaction course was monitored by H-1-NMR spectroscopy and spectrophotometric quantification. Changes in the HSA molecules were monitored by SDS-PAGE. The microenvironment of the SH group had a major effect on its reactivity and on the product yield. The reactivity of SH groups decreased in the order Cys > GSH > NAcCys. CMC did not react. The percentages of the reacted SH groups in the equilibrium state were almost equal, regardless of the ratio of thiol compound/MG (1:1, 1:2, 1:5): 38.1 +/- 0.9%; 38.2 +/- 0.7% and 39.0 +/- 0.8% for Cys; 26.5 +/- 0.6%; 26.6 +/- 2.6% and 27.4 +/- 2.5% for GSH; 10.8 +/- 0.9%; and 11.2 +/- 0.7% and 12.2 +/- 0.9% for NAcCys, respectively. Our results explain why substances containing alpha-amino-beta-mercapto-ethane as a pharmacophore are successful scavengers of MG. In equilibrium, HSA SH reacted in high percentages both with an insufficient amount and with an excess of MG (55% and 65%, respectively). An analysis of the hydrophobicity of the microenvironment of the SH group on the HSA surface showed that it could contribute to high levels of SH modification, leading to an increase in the scavenging activity of the albumin thiol.
PB  - Elsevier Ireland Ltd, Clare
T2  - Chemico-Biological Interactions
T1  - Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal
VL  - 188
IS  - 1
SP  - 21
EP  - 30
DO  - 10.1016/j.cbi.2010.07.013
ER  - 

@article{
author = "Aćimović, Jelena M. and Stanimirovic, Bojana D. and Todorović, Nina and Jovanović, Vesna B. and Mandić, Ljuba M.",
year = "2010",
abstract = "Methylglyoxal (MG), a reactive alpha-oxoaldehyde that is produced in higher quantities in diabetes, uremia, oxidative stress, aging and inflammation, reacts with the thiol groups (in addition to the amino and guanidino groups) of proteins. This causes protein modification, formation of advanced glycated end products (AGEs) and cross-linking. Low molecular mass thiols can be used as competitive targets for MG, preventing the reactions mentioned above. Therefore, this paper investigated how the microenvironment of the thiol group in low molecular mass thiols (cysteine, N-acetylcysteine (NAcCys), carboxymethylcysteine (CMC) and glutathione (GSH)) and human serum albumin (HSA) affected the thiol reaction with MG. The SH group reaction course was monitored by H-1-NMR spectroscopy and spectrophotometric quantification. Changes in the HSA molecules were monitored by SDS-PAGE. The microenvironment of the SH group had a major effect on its reactivity and on the product yield. The reactivity of SH groups decreased in the order Cys > GSH > NAcCys. CMC did not react. The percentages of the reacted SH groups in the equilibrium state were almost equal, regardless of the ratio of thiol compound/MG (1:1, 1:2, 1:5): 38.1 +/- 0.9%; 38.2 +/- 0.7% and 39.0 +/- 0.8% for Cys; 26.5 +/- 0.6%; 26.6 +/- 2.6% and 27.4 +/- 2.5% for GSH; 10.8 +/- 0.9%; and 11.2 +/- 0.7% and 12.2 +/- 0.9% for NAcCys, respectively. Our results explain why substances containing alpha-amino-beta-mercapto-ethane as a pharmacophore are successful scavengers of MG. In equilibrium, HSA SH reacted in high percentages both with an insufficient amount and with an excess of MG (55% and 65%, respectively). An analysis of the hydrophobicity of the microenvironment of the SH group on the HSA surface showed that it could contribute to high levels of SH modification, leading to an increase in the scavenging activity of the albumin thiol.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Chemico-Biological Interactions",
title = "Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal",
volume = "188",
number = "1",
pages = "21-30",
doi = "10.1016/j.cbi.2010.07.013"
}

Aćimović, J. M., Stanimirovic, B. D., Todorović, N., Jovanović, V. B.,& Mandić, L. M.. (2010). Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal. in Chemico-Biological Interactions
Elsevier Ireland Ltd, Clare., 188(1), 21-30.
https://doi.org/10.1016/j.cbi.2010.07.013

Aćimović JM, Stanimirovic BD, Todorović N, Jovanović VB, Mandić LM. Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal. in Chemico-Biological Interactions. 2010;188(1):21-30.
doi:10.1016/j.cbi.2010.07.013 .

Aćimović, Jelena M., Stanimirovic, Bojana D., Todorović, Nina, Jovanović, Vesna B., Mandić, Ljuba M., "Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal" in Chemico-Biological Interactions, 188, no. 1 (2010):21-30,
https://doi.org/10.1016/j.cbi.2010.07.013 . .

TY  - JOUR
AU  - Mandić, Ljuba
AU  - Stojanović, Srđan
AU  - Čolović, Ana
AU  - Milin, Nenad
PY  - 2000
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3889
AB  - Određivanje sadržaja glikozilovanih proteina je važno za otkrivanje i kontrolu stanja dugotrajne hiperglikemijc u dijabetesu. Cl ovom radu određivan je sadržaj glukoze vezane za proteine seruma kod obolelih od dijabetesa, spektrolotometrijskim metodama s fenol-sumpornom kiselinom (PS) i s tiobarbiturnom kiselinom (TBA). Vrednosti vezane glukoze dobijene s PS reagensom (80,6 ± 22,8 gmol glukoze/g proteina) su bile znatno više od do-bijenih s TBA metodom (3,71 ± 1,34 pmol glukoze/g proteina). Analiza faktora, koji bi mogli dovesti do ove značajne razlike, je pokazala da su više vrednosti dobijene PS metodom posledica dodatne dehidratacije ugljenih hidrata oslobođenih u toku hidrolize glikozilovanih proteina. Do dehidratacije dolazi pri izvođenju bojene reakcije s fenol-sumpornom kiselinom. Zaključeno je da, iako se osetljivost obe metode za fruktozu kao standard ne razlikuje značajno, TBA metoda je pouzdanija od PS metode i preporučuje se za kliničku praksu.
AB  - The estimation of glycosylated proteins is useful in the detection and control of long-standing hyperglycemic conditions. In this paper the content of protein-bound glucose was determined in diabetics by spectrophotometric method with phenol-sulphuric acid (PS) and with thiobarbituric acid (TBA). The amounts of protein-bound glucose obtained with the PS reagent (80.6 ± 22.8 mmol glucose/g protein) were always considerably higher than those obtained by TBA method (3.71 ± 1.34 μmol glucose/g protein). The analysis was made of parameters that might have led to such significant difference. It was shown that in the reaction with PS reagent there was an additional dehydration of carbohydrate released during the hydrolysis of glycosylated proteins. The additional dehydration was due to concentrated sulphuric acid which at higher temperature influenced chromogen formation. On the basis of the results obtained it was concluded that, although the sensitivity of the both methods for standard fructose was comparable, TBA method was more reliable than PS method. Therefore, it is recommended in clinical practice.
PB  - Društvo medicinskih biohemičara Srbije i Crne Gore i Farmaceutski fakultet, Beograd
T2  - Jugoslovenska medicinska biohemija - Yugoslav Medical Biochemistry
T1  - Odredivanje glikozilovanih proteina seruma: poredenje metoda sa tiobarbiturnom kiselinom i fenol-sumpornom kiselinom
T1  - Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays
VL  - 19
IS  - 4
SP  - 411
EP  - 416
UR  - https://hdl.handle.net/21.15107/rcub_cherry_445
ER  - 

@article{
author = "Mandić, Ljuba and Stojanović, Srđan and Čolović, Ana and Milin, Nenad",
year = "2000",
abstract = "Određivanje sadržaja glikozilovanih proteina je važno za otkrivanje i kontrolu stanja dugotrajne hiperglikemijc u dijabetesu. Cl ovom radu određivan je sadržaj glukoze vezane za proteine seruma kod obolelih od dijabetesa, spektrolotometrijskim metodama s fenol-sumpornom kiselinom (PS) i s tiobarbiturnom kiselinom (TBA). Vrednosti vezane glukoze dobijene s PS reagensom (80,6 ± 22,8 gmol glukoze/g proteina) su bile znatno više od do-bijenih s TBA metodom (3,71 ± 1,34 pmol glukoze/g proteina). Analiza faktora, koji bi mogli dovesti do ove značajne razlike, je pokazala da su više vrednosti dobijene PS metodom posledica dodatne dehidratacije ugljenih hidrata oslobođenih u toku hidrolize glikozilovanih proteina. Do dehidratacije dolazi pri izvođenju bojene reakcije s fenol-sumpornom kiselinom. Zaključeno je da, iako se osetljivost obe metode za fruktozu kao standard ne razlikuje značajno, TBA metoda je pouzdanija od PS metode i preporučuje se za kliničku praksu., The estimation of glycosylated proteins is useful in the detection and control of long-standing hyperglycemic conditions. In this paper the content of protein-bound glucose was determined in diabetics by spectrophotometric method with phenol-sulphuric acid (PS) and with thiobarbituric acid (TBA). The amounts of protein-bound glucose obtained with the PS reagent (80.6 ± 22.8 mmol glucose/g protein) were always considerably higher than those obtained by TBA method (3.71 ± 1.34 μmol glucose/g protein). The analysis was made of parameters that might have led to such significant difference. It was shown that in the reaction with PS reagent there was an additional dehydration of carbohydrate released during the hydrolysis of glycosylated proteins. The additional dehydration was due to concentrated sulphuric acid which at higher temperature influenced chromogen formation. On the basis of the results obtained it was concluded that, although the sensitivity of the both methods for standard fructose was comparable, TBA method was more reliable than PS method. Therefore, it is recommended in clinical practice.",
publisher = "Društvo medicinskih biohemičara Srbije i Crne Gore i Farmaceutski fakultet, Beograd",
journal = "Jugoslovenska medicinska biohemija - Yugoslav Medical Biochemistry",
title = "Odredivanje glikozilovanih proteina seruma: poredenje metoda sa tiobarbiturnom kiselinom i fenol-sumpornom kiselinom, Determination of serum glycosylated proteins: Comparison of thiobarbituric acid and phenol-sulphuric acid assays",
volume = "19",
number = "4",
pages = "411-416",
url = "https://hdl.handle.net/21.15107/rcub_cherry_445"
}

Mandić, L., Stojanović, S., Čolović, A.,& Milin, N.. (2000). Odredivanje glikozilovanih proteina seruma: poredenje metoda sa tiobarbiturnom kiselinom i fenol-sumpornom kiselinom. in Jugoslovenska medicinska biohemija - Yugoslav Medical Biochemistry
Društvo medicinskih biohemičara Srbije i Crne Gore i Farmaceutski fakultet, Beograd., 19(4), 411-416.
https://hdl.handle.net/21.15107/rcub_cherry_445

Mandić L, Stojanović S, Čolović A, Milin N. Odredivanje glikozilovanih proteina seruma: poredenje metoda sa tiobarbiturnom kiselinom i fenol-sumpornom kiselinom. in Jugoslovenska medicinska biohemija - Yugoslav Medical Biochemistry. 2000;19(4):411-416.
https://hdl.handle.net/21.15107/rcub_cherry_445 .

Mandić, Ljuba, Stojanović, Srđan, Čolović, Ana, Milin, Nenad, "Odredivanje glikozilovanih proteina seruma: poredenje metoda sa tiobarbiturnom kiselinom i fenol-sumpornom kiselinom" in Jugoslovenska medicinska biohemija - Yugoslav Medical Biochemistry, 19, no. 4 (2000):411-416,
https://hdl.handle.net/21.15107/rcub_cherry_445 .

TY  - CONF
AU  - Mandić, Ljuba
AU  - Stojanović, Srđan
AU  - Milin, Nenad
AU  - Čolović, Ana
PY  - 1998
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6539
AB  - In this work a new spectrophotometric method for determination of nonenzymatically scrum protein-bound carbohydrates by phenol-sulfuric acid [5] as reagent, was used. All relevant parameters as the conditions of hydrolysis of ketoamine bond between glucose and protein, and formation 5-hydroxymethylfurfuraI (5-HMF) from glucose, as well as non specific influences on the reaction 5-HMF and •phenol-sulfuric acid, were investigated. Thus the determination of protein-bound carbohydrates by phenol-sulfuric acid was found more sensitive than spectrophotometric one which use thiobarbituric acid as reagent. More significant correlation with HbAlc content, determined by ion-exchange chromatography, was found. The non-specific influences on the determination was not found. Therefore, the determination of protein-bound carbohydrates by phenol­ sulfuric acid can serve as sensitive indicator of the degree hyperglycemia in diabetes.
PB  - Association of Greek Chemists
C3  - Book of abstracts - 1st International Conference of the Chemical Societies of the South-East European Countries, June 1-4. 1999, Halkidiki, Greece
T1  - Determination of nonenzymatically protein-bound carbohydrates in serum by phenol-sulfuric acid
SP  - PO407
EP  - PO407
UR  - https://hdl.handle.net/21.15107/rcub_cer_6539
ER  - 

@conference{
author = "Mandić, Ljuba and Stojanović, Srđan and Milin, Nenad and Čolović, Ana",
year = "1998",
abstract = "In this work a new spectrophotometric method for determination of nonenzymatically scrum protein-bound carbohydrates by phenol-sulfuric acid [5] as reagent, was used. All relevant parameters as the conditions of hydrolysis of ketoamine bond between glucose and protein, and formation 5-hydroxymethylfurfuraI (5-HMF) from glucose, as well as non specific influences on the reaction 5-HMF and •phenol-sulfuric acid, were investigated. Thus the determination of protein-bound carbohydrates by phenol-sulfuric acid was found more sensitive than spectrophotometric one which use thiobarbituric acid as reagent. More significant correlation with HbAlc content, determined by ion-exchange chromatography, was found. The non-specific influences on the determination was not found. Therefore, the determination of protein-bound carbohydrates by phenol­ sulfuric acid can serve as sensitive indicator of the degree hyperglycemia in diabetes.",
publisher = "Association of Greek Chemists",
journal = "Book of abstracts - 1st International Conference of the Chemical Societies of the South-East European Countries, June 1-4. 1999, Halkidiki, Greece",
title = "Determination of nonenzymatically protein-bound carbohydrates in serum by phenol-sulfuric acid",
pages = "PO407-PO407",
url = "https://hdl.handle.net/21.15107/rcub_cer_6539"
}

Mandić, L., Stojanović, S., Milin, N.,& Čolović, A.. (1998). Determination of nonenzymatically protein-bound carbohydrates in serum by phenol-sulfuric acid. in Book of abstracts - 1st International Conference of the Chemical Societies of the South-East European Countries, June 1-4. 1999, Halkidiki, Greece
Association of Greek Chemists., PO407-PO407.
https://hdl.handle.net/21.15107/rcub_cer_6539

Mandić L, Stojanović S, Milin N, Čolović A. Determination of nonenzymatically protein-bound carbohydrates in serum by phenol-sulfuric acid. in Book of abstracts - 1st International Conference of the Chemical Societies of the South-East European Countries, June 1-4. 1999, Halkidiki, Greece. 1998;:PO407-PO407.
https://hdl.handle.net/21.15107/rcub_cer_6539 .

Mandić, Ljuba, Stojanović, Srđan, Milin, Nenad, Čolović, Ana, "Determination of nonenzymatically protein-bound carbohydrates in serum by phenol-sulfuric acid" in Book of abstracts - 1st International Conference of the Chemical Societies of the South-East European Countries, June 1-4. 1999, Halkidiki, Greece (1998):PO407-PO407,
https://hdl.handle.net/21.15107/rcub_cer_6539 .

TY  - CONF
AU  - Mandić, Ljuba
AU  - Đurđić, Vidosava
AU  - Borozan, Sunčica
AU  - Stojanović, Srđan
PY  - 1990
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6552
AB  - Insulinoma, pancreas tumors lead to the increased insulin secretion, glucose consump­tion and the hypoglycemia emergence. The changes of erythrocyte metabolism in hypoglycemia have not been studied so far.
To explain the influence of hypoglycemia on erythrocyte metabolism the activities of erythrocyte enzymes and the content of hemo­globin derivates were analyzed. More precise identification of some modified hemoglobins was carried out; and their contents we­re analysed too.The physiological importance and practical application of results remains to be solved.
PB  - The Federation of European Biochemical Societies (FEBS)
C3  - Abstracts - 20th Meeting of the Federation of European Biochemical Societies, August 19-24, 1990, Budapest, Hungary
T1  - The changes in erythrocyte metabolism in hypoglycemia
SP  - 149
EP  - 149
UR  - https://hdl.handle.net/21.15107/rcub_cer_6552
ER  - 

@conference{
author = "Mandić, Ljuba and Đurđić, Vidosava and Borozan, Sunčica and Stojanović, Srđan",
year = "1990",
abstract = "Insulinoma, pancreas tumors lead to the increased insulin secretion, glucose consump­tion and the hypoglycemia emergence. The changes of erythrocyte metabolism in hypoglycemia have not been studied so far.
To explain the influence of hypoglycemia on erythrocyte metabolism the activities of erythrocyte enzymes and the content of hemo­globin derivates were analyzed. More precise identification of some modified hemoglobins was carried out; and their contents we­re analysed too.The physiological importance and practical application of results remains to be solved.",
publisher = "The Federation of European Biochemical Societies (FEBS)",
journal = "Abstracts - 20th Meeting of the Federation of European Biochemical Societies, August 19-24, 1990, Budapest, Hungary",
title = "The changes in erythrocyte metabolism in hypoglycemia",
pages = "149-149",
url = "https://hdl.handle.net/21.15107/rcub_cer_6552"
}

Mandić, L., Đurđić, V., Borozan, S.,& Stojanović, S.. (1990). The changes in erythrocyte metabolism in hypoglycemia. in Abstracts - 20th Meeting of the Federation of European Biochemical Societies, August 19-24, 1990, Budapest, Hungary
The Federation of European Biochemical Societies (FEBS)., 149-149.
https://hdl.handle.net/21.15107/rcub_cer_6552

Mandić L, Đurđić V, Borozan S, Stojanović S. The changes in erythrocyte metabolism in hypoglycemia. in Abstracts - 20th Meeting of the Federation of European Biochemical Societies, August 19-24, 1990, Budapest, Hungary. 1990;:149-149.
https://hdl.handle.net/21.15107/rcub_cer_6552 .

Mandić, Ljuba, Đurđić, Vidosava, Borozan, Sunčica, Stojanović, Srđan, "The changes in erythrocyte metabolism in hypoglycemia" in Abstracts - 20th Meeting of the Federation of European Biochemical Societies, August 19-24, 1990, Budapest, Hungary (1990):149-149,
https://hdl.handle.net/21.15107/rcub_cer_6552 .