TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4893
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 

@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}

Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8

Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .

Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .

TY  - CHAP
AU  - Nikolić, Milan
AU  - Minić, Simeon L.
AU  - Mačvanin, Mirjana T.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
AU  - Jacob-Lopes, Eduardo
AU  - Queiroz, Maria Isabel
AU  - Zepka, Leila Queiroz
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4892
AB  - The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.
PB  - Springer International Publishing
T2  - Pigments from Microalgae Handbook
T1  - Analytical Protocols in Phycobiliproteins Analysis
SP  - 179
EP  - 201
DO  - 10.1007/978-3-030-50971-2_8
ER  - 

@inbook{
author = "Nikolić, Milan and Minić, Simeon L. and Mačvanin, Mirjana T. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja and Jacob-Lopes, Eduardo and Queiroz, Maria Isabel and Zepka, Leila Queiroz",
year = "2020",
abstract = "The aim of this chapter is to review and discuss methodology and protocols in the analysis of phycobiliproteins (phycocyanins, allophycocyanins, and phycoerythrins) and their chromophores. Due to the presence of multiple covalently bound open-chain tetrapyrrole chromophores, phycobiliproteins are colored and strongly fluorescent molecules, with high absorption coefficients (105 to 106) and excellent fluorescent quantum yield (0.51 up to 0.98). Therefore, a vast number of methods for phycobiliproteins analysis is based on these spectral characteristics, whereas assessment of their bioactivity is related to their exceptional redox and metal-chelating properties. This chapter is dedicated to methods used for isolation and purification, structure analysis, physicochemical properties and stability characterization, quantification, as well as in vitro and in vivo biological activities evaluation. In addition, emerging approaches related to phycobiliproteins analysis are also reviewed including interactions with other biomolecules and ions and identification of phycobiliprotein (chromo)peptides by mass spectrometry.",
publisher = "Springer International Publishing",
journal = "Pigments from Microalgae Handbook",
booktitle = "Analytical Protocols in Phycobiliproteins Analysis",
pages = "179-201",
doi = "10.1007/978-3-030-50971-2_8"
}

Nikolić, M., Minić, S. L., Mačvanin, M. T., Stanić-Vučinić, D., Ćirković-Veličković, T., Jacob-Lopes, E., Queiroz, M. I.,& Zepka, L. Q.. (2020). Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook
Springer International Publishing., 179-201.
https://doi.org/10.1007/978-3-030-50971-2_8

Nikolić M, Minić SL, Mačvanin MT, Stanić-Vučinić D, Ćirković-Veličković T, Jacob-Lopes E, Queiroz MI, Zepka LQ. Analytical Protocols in Phycobiliproteins Analysis. in Pigments from Microalgae Handbook. 2020;:179-201.
doi:10.1007/978-3-030-50971-2_8 .

Nikolić, Milan, Minić, Simeon L., Mačvanin, Mirjana T., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, Jacob-Lopes, Eduardo, Queiroz, Maria Isabel, Zepka, Leila Queiroz, "Analytical Protocols in Phycobiliproteins Analysis" in Pigments from Microalgae Handbook (2020):179-201,
https://doi.org/10.1007/978-3-030-50971-2_8 . .

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://cherry.chem.bg.ac.rs/handle/123456789/3333
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.
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  - 1
EP  - 7
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.",
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 = "1-7",
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, 311, 1-7.
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;311:1-7.
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):1-7,
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - DATA
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://cherry.chem.bg.ac.rs/handle/123456789/3335
T2  - Chemico-Biological Interactions
T1  - Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. 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. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3335
ER  - 

@misc{
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",
journal = "Chemico-Biological Interactions",
title = "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. 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. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3335"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. 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. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions.
https://hdl.handle.net/21.15107/rcub_cherry_3335

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. 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. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3335 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. 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. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787" in Chemico-Biological Interactions (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3335 .

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://cherry.chem.bg.ac.rs/handle/123456789/3865
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
IS  - 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",
number = "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, no. 108787 (2019),
https://doi.org/10.1016/j.cbi.2019.108787 . .