Jovanović, Vesna B.

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orcid::0000-0001-9356-0813
  • Jovanović, Vesna B. (6)

Author's Bibliography

Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics

Lujić, Tamara; Gligorijević, Nikola; Jovanović, Vesna B.; Aćimović, Jelena; Mitić, Dragana; Vasović, Tamara; Stojadinović, Marija; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Italian Proteomics Association, 2023)

TY  - CONF
AU  - Lujić, Tamara
AU  - Gligorijević, Nikola
AU  - Jovanović, Vesna B.
AU  - Aćimović, Jelena
AU  - Mitić, Dragana
AU  - Vasović, Tamara
AU  - Stojadinović, Marija
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7473
AB  - Microplastics is abundant in the environment, food and beverages and get ingested by humans.
Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent
hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft
corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin
(OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was
aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to
polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified
allergens and egg white proteins. After establishment of binding equilibrium, soft and hard
corona were separated and analyzed by SDS PAGE, followed by identification of bound
proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and
hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard
corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or
fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity
for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant
under similar conditions. BLG is compact globular protein with lower level of exposed
hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace
amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white
protein extract OVA forms both SC and HC on microplastics, being the dominant protein of
hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona.
Both proteins are known for their strong bioactivity and represent a small fraction of total egg
white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg
white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing
effect of strong binding to microplastics may change functional characteristics of allergens and
bioactive proteins of foods and should be further investigated in functional assays.
PB  - Italian Proteomics Association
C3  - XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy
T1  - Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cer_7473
ER  - 
@conference{
author = "Lujić, Tamara and Gligorijević, Nikola and Jovanović, Vesna B. and Aćimović, Jelena and Mitić, Dragana and Vasović, Tamara and Stojadinović, Marija and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "Microplastics is abundant in the environment, food and beverages and get ingested by humans.
Its complex interplay with proteins lead to formation of corona. Tightly bound proteins represent
hard corona, while weaker binding partners are found in soft corona. Separation of hard and soft
corona of allergenic proteins of shrimps, eggs and cow’s milk, tropomyosin (TPM), ovalbumin
(OVA) and beta-lactoglobulin (BLG) and identification of binding partners by proteomics was
aim of our study.
Allergenic proteins were purified from egg white, shrimps and cow’s milk. Binding to
polyethylene terephthalate microplastics (PET) (70-100 m) was probed at pH 7 for purified
allergens and egg white proteins. After establishment of binding equilibrium, soft and hard
corona were separated and analyzed by SDS PAGE, followed by identification of bound
proteins by nanoLC-HRMS. Binding of all allergenic proteins was observed in both soft and
hard corona. Soft corona contains exclusively intact, full length OVA, TPM and BLG. Hard
corona is enriched for truncated OVA and oligomers of TPM. OVA fragments are partially or
fully enfolded and have higher level of exposed hydrophobic patches resulting in higher affinity
for PET microplastics. In comparison to OVA and TPM, hard corona of BLG is less abundant
under similar conditions. BLG is compact globular protein with lower level of exposed
hydrophobic patches in comparison to ovalbumin and tropomyosin. In hard corona, trace
amounts of contaminating alfa-lactalbumin become enriched. In the presence of egg white
protein extract OVA forms both SC and HC on microplastics, being the dominant protein of
hard corona (with ovotransferrin). Lysozyme and ovomucin are present only in hard corona.
Both proteins are known for their strong bioactivity and represent a small fraction of total egg
white proteins.
Our results show that allergenic proteins form hard corona on PET microplastics. Among egg
white proteins, minor proteins such as lysozyme and ovomucin become enriched. Denaturing
effect of strong binding to microplastics may change functional characteristics of allergens and
bioactive proteins of foods and should be further investigated in functional assays.",
publisher = "Italian Proteomics Association",
journal = "XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy",
title = "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cer_7473"
}
Lujić, T., Gligorijević, N., Jovanović, V. B., Aćimović, J., Mitić, D., Vasović, T., Stojadinović, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2023). Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy
Italian Proteomics Association., 11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473
Lujić T, Gligorijević N, Jovanović VB, Aćimović J, Mitić D, Vasović T, Stojadinović M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics. in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy. 2023;:11-11.
https://hdl.handle.net/21.15107/rcub_cer_7473 .
Lujić, Tamara, Gligorijević, Nikola, Jovanović, Vesna B., Aćimović, Jelena, Mitić, Dragana, Vasović, Tamara, Stojadinović, Marija, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic insight into allergenic food corona on polyethylene terephthalate microplastics" in XVII International Italian Proteomics Association Annual Meeting in partnership with the Hellenic Proteomics Society and Serbian Proteomics Association, "Proteomics and Metabolomics towards Global Health", November 29th-December 1st, 2023, Ospedale Isola Tiberina - Gemelli Isola,  Roma, Italy (2023):11-11,
https://hdl.handle.net/21.15107/rcub_cer_7473 .

Evaluation of the universality of NMR metabolic fingerprints of schizophrenia

Simić, Katarina; Todorović, Nina; Miladinović, Zoran; Ivanović, Stefan; Trifunović, Snežana; Vujisić, Ljubodrag; Tešević, Vele; Jovanović, Vesna B.; Avramović, Nataša; Gavrilović, Aleksandra; Jovanović, Silvana; Costa, Tássia Brena Barroso Carneiro; Huan Liu, Leticia; Barros, Pedro; Stanišić, Danijela; Mandić, Boris; Tasić, Ljubica

(University of Belgrade - Faculty of Chemistry, 2019)

TY  - CONF
AU  - Simić, Katarina
AU  - Todorović, Nina
AU  - Miladinović, Zoran
AU  - Ivanović, Stefan
AU  - Trifunović, Snežana
AU  - Vujisić, Ljubodrag
AU  - Tešević, Vele
AU  - Jovanović, Vesna B.
AU  - Avramović, Nataša
AU  - Gavrilović, Aleksandra
AU  - Jovanović, Silvana
AU  - Costa, Tássia Brena Barroso Carneiro
AU  - Huan Liu, Leticia
AU  - Barros, Pedro
AU  - Stanišić, Danijela
AU  - Mandić, Boris
AU  - Tasić, Ljubica
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7536
AB  - Schizophrenia (SCZ) is a very disabling mental disorder whose molecular basis is a combination of many factors still not completely understood, with a diagnosis based on observed behavior, the person's reported experiences and reports of others that are familiar with the person, with no objective test. Also, up to date, there are no reliable markers for monitoring the SCZ. NMR-metabolomics [1] reported in 2017 bring some of the possible markers from blood serum of SCZ individuals linked strongly with known dopamine, glutamate and GABA dysfunction in SCZ. As to verify if these findings are universal, we have compared the SCZ patients from geographically different environments and cited interesting SCZ characteristics.  
The first set of samples was collected in Belgrade, Serbia. 14 mental health patients (50% male) with 52.86 ± 7.27 years of age had a confirmed diagnosis of SCZ. The control group of 13 healthy individuals (69% male) had none of psychotic disorders, and individuals were 23.07 ± 2.79 years of age. Blood serum samples were collected and prepared for the analysis following the published methodology [1, 2]. NMR spectra were measured on a Bruker AVANCE III spectrometer (500.26 MHz for 1H). The spectra were acquired at 298 K with 128 scans and 32 k. The serum samples were prepared and measured as triplicates.  
On the other side, the group of individuals from Brazil that was matched in number, age, gender and history of mental illness with individuals from Serbia was previously described [1].  
1H NMR spectra were phase and baseline corrected using MestreNova and the lactate doublet was used as the chemical shift reference. The data were binned (0.005 ppm) in a spectral range 0.50 - 9.00 ppm, while the residual HDO peak (4.50-5.00 ppm) was excluded. Then, the data were normalized by the sum equal to 1000, the variables were mean centered and PCA and PLS-DA were performed using MATLAB.  
It was shown that the mental health patients have clearly different blood serum metabolites when compared to the healthy ones independently from where the samples were obtained with almost identical marker set. Also, it was shown that the samples are different metabolically when Brazilian and Serbian samples were compared. 
1] L. Tasic et al., Schizophrenia Research 2017, 185, 182.
[2] J. Pontes et al., Analytical Methods 2017, 9, 1078.
PB  - University of Belgrade - Faculty of  Chemistry
PB  - Institute of Chemistry, Technology and Metallurgy, National Institute
C3  - Book of Abstracts - 21st Central European NMR Symposium &  Bruker Users Meeting, 21st CEUM, September 4-5, 2019, Belgrade, Serbia
T1  - Evaluation of the universality of NMR metabolic fingerprints of schizophrenia
SP  - 31
EP  - 32
UR  - https://hdl.handle.net/21.15107/rcub_cer_7536
ER  - 
@conference{
author = "Simić, Katarina and Todorović, Nina and Miladinović, Zoran and Ivanović, Stefan and Trifunović, Snežana and Vujisić, Ljubodrag and Tešević, Vele and Jovanović, Vesna B. and Avramović, Nataša and Gavrilović, Aleksandra and Jovanović, Silvana and Costa, Tássia Brena Barroso Carneiro and Huan Liu, Leticia and Barros, Pedro and Stanišić, Danijela and Mandić, Boris and Tasić, Ljubica",
year = "2019",
abstract = "Schizophrenia (SCZ) is a very disabling mental disorder whose molecular basis is a combination of many factors still not completely understood, with a diagnosis based on observed behavior, the person's reported experiences and reports of others that are familiar with the person, with no objective test. Also, up to date, there are no reliable markers for monitoring the SCZ. NMR-metabolomics [1] reported in 2017 bring some of the possible markers from blood serum of SCZ individuals linked strongly with known dopamine, glutamate and GABA dysfunction in SCZ. As to verify if these findings are universal, we have compared the SCZ patients from geographically different environments and cited interesting SCZ characteristics.  
The first set of samples was collected in Belgrade, Serbia. 14 mental health patients (50% male) with 52.86 ± 7.27 years of age had a confirmed diagnosis of SCZ. The control group of 13 healthy individuals (69% male) had none of psychotic disorders, and individuals were 23.07 ± 2.79 years of age. Blood serum samples were collected and prepared for the analysis following the published methodology [1, 2]. NMR spectra were measured on a Bruker AVANCE III spectrometer (500.26 MHz for 1H). The spectra were acquired at 298 K with 128 scans and 32 k. The serum samples were prepared and measured as triplicates.  
On the other side, the group of individuals from Brazil that was matched in number, age, gender and history of mental illness with individuals from Serbia was previously described [1].  
1H NMR spectra were phase and baseline corrected using MestreNova and the lactate doublet was used as the chemical shift reference. The data were binned (0.005 ppm) in a spectral range 0.50 - 9.00 ppm, while the residual HDO peak (4.50-5.00 ppm) was excluded. Then, the data were normalized by the sum equal to 1000, the variables were mean centered and PCA and PLS-DA were performed using MATLAB.  
It was shown that the mental health patients have clearly different blood serum metabolites when compared to the healthy ones independently from where the samples were obtained with almost identical marker set. Also, it was shown that the samples are different metabolically when Brazilian and Serbian samples were compared. 
1] L. Tasic et al., Schizophrenia Research 2017, 185, 182.
[2] J. Pontes et al., Analytical Methods 2017, 9, 1078.",
publisher = "University of Belgrade - Faculty of  Chemistry, Institute of Chemistry, Technology and Metallurgy, National Institute",
journal = "Book of Abstracts - 21st Central European NMR Symposium &  Bruker Users Meeting, 21st CEUM, September 4-5, 2019, Belgrade, Serbia",
title = "Evaluation of the universality of NMR metabolic fingerprints of schizophrenia",
pages = "31-32",
url = "https://hdl.handle.net/21.15107/rcub_cer_7536"
}
Simić, K., Todorović, N., Miladinović, Z., Ivanović, S., Trifunović, S., Vujisić, L., Tešević, V., Jovanović, V. B., Avramović, N., Gavrilović, A., Jovanović, S., Costa, T. B. B. C., Huan Liu, L., Barros, P., Stanišić, D., Mandić, B.,& Tasić, L.. (2019). Evaluation of the universality of NMR metabolic fingerprints of schizophrenia. in Book of Abstracts - 21st Central European NMR Symposium &  Bruker Users Meeting, 21st CEUM, September 4-5, 2019, Belgrade, Serbia
University of Belgrade - Faculty of  Chemistry., 31-32.
https://hdl.handle.net/21.15107/rcub_cer_7536
Simić K, Todorović N, Miladinović Z, Ivanović S, Trifunović S, Vujisić L, Tešević V, Jovanović VB, Avramović N, Gavrilović A, Jovanović S, Costa TBBC, Huan Liu L, Barros P, Stanišić D, Mandić B, Tasić L. Evaluation of the universality of NMR metabolic fingerprints of schizophrenia. in Book of Abstracts - 21st Central European NMR Symposium &  Bruker Users Meeting, 21st CEUM, September 4-5, 2019, Belgrade, Serbia. 2019;:31-32.
https://hdl.handle.net/21.15107/rcub_cer_7536 .
Simić, Katarina, Todorović, Nina, Miladinović, Zoran, Ivanović, Stefan, Trifunović, Snežana, Vujisić, Ljubodrag, Tešević, Vele, Jovanović, Vesna B., Avramović, Nataša, Gavrilović, Aleksandra, Jovanović, Silvana, Costa, Tássia Brena Barroso Carneiro, Huan Liu, Leticia, Barros, Pedro, Stanišić, Danijela, Mandić, Boris, Tasić, Ljubica, "Evaluation of the universality of NMR metabolic fingerprints of schizophrenia" in Book of Abstracts - 21st Central European NMR Symposium &  Bruker Users Meeting, 21st CEUM, September 4-5, 2019, Belgrade, Serbia (2019):31-32,
https://hdl.handle.net/21.15107/rcub_cer_7536 .

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

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(Elsevier, 2019)

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 . .
2
2

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

Uzelac, Tamara N.; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Mačvanin, Mirjana T.; Nikolić, Milan; Mandić, Ljuba M.; Jovanović, Vesna B.

(Elsevier, 2019)

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 . .
2
2

Non-covalent interactions across subunit interfaces in Sm proteins

Zarić, Božidarka; Jovanović, Vesna B.; Stojanović, Srđan

(Academic Press Ltd- Elsevier Science Ltd, London, 2011)

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Jovanović, Vesna B.
AU  - Stojanović, Srđan
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/924
AB  - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Theoretical Biology
T1  - Non-covalent interactions across subunit interfaces in Sm proteins
VL  - 271
IS  - 1
SP  - 18
EP  - 26
DO  - 10.1016/j.jtbi.2010.11.025
ER  - 
@article{
author = "Zarić, Božidarka and Jovanović, Vesna B. and Stojanović, Srđan",
year = "2011",
abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Theoretical Biology",
title = "Non-covalent interactions across subunit interfaces in Sm proteins",
volume = "271",
number = "1",
pages = "18-26",
doi = "10.1016/j.jtbi.2010.11.025"
}
Zarić, B., Jovanović, V. B.,& Stojanović, S.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology
Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26.
https://doi.org/10.1016/j.jtbi.2010.11.025
Zarić B, Jovanović VB, Stojanović S. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26.
doi:10.1016/j.jtbi.2010.11.025 .
Zarić, Božidarka, Jovanović, Vesna B., Stojanović, Srđan, "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26,
https://doi.org/10.1016/j.jtbi.2010.11.025 . .
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Influence of the microenvironment of thiol groups in low molecular mass thiols and serum albumin on the reaction with methylglyoxal

Aćimović, Jelena M.; Stanimirovic, Bojana D.; Todorović, Nina; Jovanović, Vesna B.; Mandić, Ljuba M.

(Elsevier Ireland Ltd, Clare, 2010)

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 . .
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