Gligorijević, Nikola

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Authority KeyName Variants
orcid::0000-0002-8691-2486
  • Gligorijević, Nikola (16)
Projects
Structural characterisation of the insulin-like growth factor (IGF) binding proteins and IGF receptors, their interactions with other physiological molecules and alterations in metabolic disorders Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200019 (University of Belgrade, Institute for the Application of Nuclear Energy - INEP)
[SK-SRB-2016-0023] Slovak Grant Agency for Science-VEGA [2/0162/14]
Belgian Special Research Fund BOF STG, grant number 01N01718. ICGEB research [CRP/YUG11-02]
ICGEB Research Grant [CRP/YUG11-02] Ministarstvo prosvete, nauke i tehnološkog razvoja Republike Srbije, Ugovor br. 451-03-68/2020-14/2019
Serbian Academy of Sciences and Arts, grant number F-26. The Serbian Academy of Sciences and Arts, grant number F-26

Author's Bibliography

Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability

Gligorijević, Nikola; Stanić-Vučinić, Dragana; Radomirović, Mirjana; Stojadinović, Marija M.; Khulal, Urmila; Nedić, Olgica; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://www.mdpi.com/1420-3049/26/10/2834
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4552
AB  - Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
PB  - MDPI
T2  - Molecules
T1  - Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability
VL  - 26
IS  - 10
SP  - 2834
DO  - 10.3390/molecules26102834
ER  - 
@article{
author = "Gligorijević, Nikola and Stanić-Vučinić, Dragana and Radomirović, Mirjana and Stojadinović, Marija M. and Khulal, Urmila and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.",
publisher = "MDPI",
journal = "Molecules",
title = "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability",
volume = "26",
number = "10",
pages = "2834",
doi = "10.3390/molecules26102834"
}
Gligorijević, N., Stanić-Vučinić, D., Radomirović, M., Stojadinović, M. M., Khulal, U., Nedić, O.,& Ćirković-Veličković, T.. (2021). Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules
MDPI., 26(10), 2834.
https://doi.org/10.3390/molecules26102834
Gligorijević N, Stanić-Vučinić D, Radomirović M, Stojadinović MM, Khulal U, Nedić O, Ćirković-Veličković T. Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules. 2021;26(10):2834.
doi:10.3390/molecules26102834 .
Gligorijević, Nikola, Stanić-Vučinić, Dragana, Radomirović, Mirjana, Stojadinović, Marija M., Khulal, Urmila, Nedić, Olgica, Ćirković-Veličković, Tanja, "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability" in Molecules, 26, no. 10 (2021):2834,
https://doi.org/10.3390/molecules26102834 . .
1
2

Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity

Gligorijević, Nikola; Minić, Simeon; Radibratović, Milica; Papadimitriou, Vassiliki; Nedić, Olgica; Sotiroudis, Theodore G.; Nikolić, Milan R.

(Elsevier, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Radibratović, Milica
AU  - Papadimitriou, Vassiliki
AU  - Nedić, Olgica
AU  - Sotiroudis, Theodore G.
AU  - Nikolić, Milan R.
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S1386142521000597
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4486
AB  - Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.
PB  - Elsevier
T2  - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
T2  - Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
T1  - Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity
VL  - 251
SP  - 119483
DO  - 10.1016/j.saa.2021.119483
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon and Radibratović, Milica and Papadimitriou, Vassiliki and Nedić, Olgica and Sotiroudis, Theodore G. and Nikolić, Milan R.",
year = "2021",
abstract = "Phycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.",
publisher = "Elsevier",
journal = "Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy",
title = "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity",
volume = "251",
pages = "119483",
doi = "10.1016/j.saa.2021.119483"
}
Gligorijević, N., Minić, S., Radibratović, M., Papadimitriou, V., Nedić, O., Sotiroudis, T. G.,& Nikolić, M. R.. (2021). Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
Elsevier., 251, 119483.
https://doi.org/10.1016/j.saa.2021.119483
Gligorijević N, Minić S, Radibratović M, Papadimitriou V, Nedić O, Sotiroudis TG, Nikolić MR. Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2021;251:119483.
doi:10.1016/j.saa.2021.119483 .
Gligorijević, Nikola, Minić, Simeon, Radibratović, Milica, Papadimitriou, Vassiliki, Nedić, Olgica, Sotiroudis, Theodore G., Nikolić, Milan R., "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity" in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 251 (2021):119483,
https://doi.org/10.1016/j.saa.2021.119483 . .
1

Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein

Šunderić, Miloš; Vasović, Tamara; Milčić, Miloš; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan R.; Gligorijević, Nikola

(Elsevier, 2021)

TY  - JOUR
AU  - Šunderić, Miloš
AU  - Vasović, Tamara
AU  - Milčić, Miloš
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan R.
AU  - Gligorijević, Nikola
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021009284
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4538
AB  - In this study, the interaction between clozapine, an atypical antipsychotic drug, and alpha-2-macroglobulin (α2M), a multipurpose anti-proteinase, was investigated under simulated (patho) physiological conditions using multiple spectroscopic techniques and molecular modeling. It was found that α2M binds clozapine with a moderate affinity (the binding constant of 0.9 × 105 M−1 at 37 °C). The preferable binding site for both clozapine's atropisomers was revealed to be a large pocket at the interface of C and D monomer subunits of the protein. Hydrogen bonds and the hydrophobic effect were proposed as dominant forces in complex formation. The binding of clozapine did not induce significant conformational change of the protein, as confirmed by virtually unaltered α2M secondary structure and anti-proteinase activity. However, both clozapine and α2M shielded each other from the deleterious influence of strong oxidants: sodium hypochlorite and 2,2′-azobis-2-methyl-propanimidamide dihydrochloride (AAPH). Moreover, clozapine in a concentration range that is usually targeted in the plasma during patients' treatment effectively protected the anti-proteinase activity of α2M under AAPH-induced free radical overproduction. Our results suggest that the cooperation between α2M and clozapine may be a path by which these two molecules synergistically protect neural tissue against injury caused by disturbed proteostasis or oxidative stress.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein
VL  - 183
SP  - 502
EP  - 512
DO  - 10.1016/j.ijbiomac.2021.04.155
ER  - 
@article{
author = "Šunderić, Miloš and Vasović, Tamara and Milčić, Miloš and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan R. and Gligorijević, Nikola",
year = "2021",
abstract = "In this study, the interaction between clozapine, an atypical antipsychotic drug, and alpha-2-macroglobulin (α2M), a multipurpose anti-proteinase, was investigated under simulated (patho) physiological conditions using multiple spectroscopic techniques and molecular modeling. It was found that α2M binds clozapine with a moderate affinity (the binding constant of 0.9 × 105 M−1 at 37 °C). The preferable binding site for both clozapine's atropisomers was revealed to be a large pocket at the interface of C and D monomer subunits of the protein. Hydrogen bonds and the hydrophobic effect were proposed as dominant forces in complex formation. The binding of clozapine did not induce significant conformational change of the protein, as confirmed by virtually unaltered α2M secondary structure and anti-proteinase activity. However, both clozapine and α2M shielded each other from the deleterious influence of strong oxidants: sodium hypochlorite and 2,2′-azobis-2-methyl-propanimidamide dihydrochloride (AAPH). Moreover, clozapine in a concentration range that is usually targeted in the plasma during patients' treatment effectively protected the anti-proteinase activity of α2M under AAPH-induced free radical overproduction. Our results suggest that the cooperation between α2M and clozapine may be a path by which these two molecules synergistically protect neural tissue against injury caused by disturbed proteostasis or oxidative stress.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein",
volume = "183",
pages = "502-512",
doi = "10.1016/j.ijbiomac.2021.04.155"
}
Šunderić, M., Vasović, T., Milčić, M., Miljević, Č., Nedić, O., Nikolić, M. R.,& Gligorijević, N.. (2021). Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein. in International Journal of Biological Macromolecules
Elsevier., 183, 502-512.
https://doi.org/10.1016/j.ijbiomac.2021.04.155
Šunderić M, Vasović T, Milčić M, Miljević Č, Nedić O, Nikolić MR, Gligorijević N. Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein. in International Journal of Biological Macromolecules. 2021;183:502-512.
doi:10.1016/j.ijbiomac.2021.04.155 .
Šunderić, Miloš, Vasović, Tamara, Milčić, Miloš, Miljević, Čedo, Nedić, Olgica, Nikolić, Milan R., Gligorijević, Nikola, "Antipsychotic clozapine binding to alpha-2-macroglobulin protects interacting partners against oxidation and preserves the anti-proteinase activity of the protein" in International Journal of Biological Macromolecules, 183 (2021):502-512,
https://doi.org/10.1016/j.ijbiomac.2021.04.155 . .
2

Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155.

Šunderić, Miloš; Vasović, Tamara; Milčić, Miloš; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan R.; Gligorijević, Nikola

(Elsevier, 2021)

TY  - DATA
AU  - Šunderić, Miloš
AU  - Vasović, Tamara
AU  - Milčić, Miloš
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan R.
AU  - Gligorijević, Nikola
PY  - 2021
UR  - https://www.sciencedirect.com/science/article/pii/S0141813021009284
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4541
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155.
DO  - 10.1016/j.ijbiomac.2021.04.155
ER  - 
@misc{
author = "Šunderić, Miloš and Vasović, Tamara and Milčić, Miloš and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan R. and Gligorijević, Nikola",
year = "2021",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155.",
doi = "10.1016/j.ijbiomac.2021.04.155"
}
Šunderić, M., Vasović, T., Milčić, M., Miljević, Č., Nedić, O., Nikolić, M. R.,& Gligorijević, N.. (2021). Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155.. in International Journal of Biological Macromolecules
Elsevier..
https://doi.org/10.1016/j.ijbiomac.2021.04.155
Šunderić M, Vasović T, Milčić M, Miljević Č, Nedić O, Nikolić MR, Gligorijević N. Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155.. in International Journal of Biological Macromolecules. 2021;.
doi:10.1016/j.ijbiomac.2021.04.155 .
Šunderić, Miloš, Vasović, Tamara, Milčić, Miloš, Miljević, Čedo, Nedić, Olgica, Nikolić, Milan R., Gligorijević, Nikola, "Supplementary data for the article: Šunderić, M.; Vasović, T.; Milčić, M.; Miljević, Č.; Nedić, O.; Nikolić, M. R.; Gligorijević, N. Antipsychotic Clozapine Binding to Alpha-2-Macroglobulin Protects Interacting Partners against Oxidation and Preserves the Anti-Proteinase Activity of the Protein. International Journal of Biological Macromolecules 2021, 183, 502–512. https://doi.org/10.1016/j.ijbiomac.2021.04.155." in International Journal of Biological Macromolecules (2021),
https://doi.org/10.1016/j.ijbiomac.2021.04.155 . .
2

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević, Nikola; Radomirović, Mirjana Ž.; Rajković, Andreja; Nedić, Olgica; Ćirković-Veličković, Tanja

(Multidisciplinary Digital Publishing Institute (MDPI), 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4235
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 
@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}
Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780
Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods. 2020;9(6):780.
doi:10.3390/foods9060780 .
Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" in Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 . .
2
2
1

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3886
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M.. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. in International Journal of Biological Macromolecules
Elsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. in International Journal of Biological Macromolecules. 2020;154:142-149.
doi:10.1016/j.ijbiomac.2020.03.119 .
Gligorijević, Nikola, Vasović, Tamara, Lević, Steva M., Miljević, Čedo, Nedić, Olgica, Nikolić, Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" in International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 . .
2
2
3

Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation

Gligorijević, Nikola; Vasović, Tamara; Lević, Steva M.; Miljević, Čedo; Nedić, Olgica; Nikolić, Milan

(Elsevier, 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Vasović, Tamara
AU  - Lević, Steva M.
AU  - Miljević, Čedo
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3896
AB  - Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation
VL  - 154
SP  - 142
EP  - 149
DO  - 10.1016/j.ijbiomac.2020.03.119
ER  - 
@article{
author = "Gligorijević, Nikola and Vasović, Tamara and Lević, Steva M. and Miljević, Čedo and Nedić, Olgica and Nikolić, Milan",
year = "2020",
abstract = "Clozapine is an atypical antipsychotic used for the treatment of schizophrenia. The prescribed target daily doses may reach 900 mg. Literature studies report a connection between clozapine usage and thrombosis development. Our in vitro study aimed to provide insight into molecular bases of this observation, investigating clozapine binding to fibrinogen, the main plasma protein involved in hemostasis. Fibrinogen/clozapine interaction was confirmed by protein fluorescence quenching, with an affinity constant of 1.7 × 105 M−1. Direct interactions did not affect the structure of fibrinogen, nor fibrinogen melting temperature. Clozapine binding affected fibrin formation by reducing coagulation speed and thickness of fibrin fibers suggesting that in the presence of clozapine, fibrinogen may acquire thrombogenic characteristics. Although no difference in fibrin gel porosity was detected, other factors present in the blood may act synergistically with altered fibrin formation to modify fibrin clot, thus increasing the risk for development of thrombosis in patients on clozapine treatment. ORAC and HORAC assays showed that clozapine reduced free radical-induced oxidation of fibrinogen. All observed effects of clozapine on fibrinogen are dose-dependent, with the effect on fibrin formation being more pronounced.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation",
volume = "154",
pages = "142-149",
doi = "10.1016/j.ijbiomac.2020.03.119"
}
Gligorijević, N., Vasović, T., Lević, S. M., Miljević, Č., Nedić, O.,& Nikolić, M.. (2020). Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. in International Journal of Biological Macromolecules
Elsevier., 154, 142-149.
https://doi.org/10.1016/j.ijbiomac.2020.03.119
Gligorijević N, Vasović T, Lević SM, Miljević Č, Nedić O, Nikolić M. Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation. in International Journal of Biological Macromolecules. 2020;154:142-149.
doi:10.1016/j.ijbiomac.2020.03.119 .
Gligorijević, Nikola, Vasović, Tamara, Lević, Steva M., Miljević, Čedo, Nedić, Olgica, Nikolić, Milan, "Atypical antipsychotic clozapine binds fibrinogen and affects fibrin formation" in International Journal of Biological Macromolecules, 154 (2020):142-149,
https://doi.org/10.1016/j.ijbiomac.2020.03.119 . .
2
2
3

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2824
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules. 2019;128:74-79.
doi:10.1016/j.ijbiomac.2019.01.124 .
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" in International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 . .
6
6
6

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2825
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. in International Journal of Biological Macromolecules. 2019;128:74-79.
doi:10.1016/j.ijbiomac.2019.01.124 .
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" in International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 . .
6
6
6

Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - DATA
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2937
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
ER  - 
@misc{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2019). Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. in International Journal of Biological Macromolecules.
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. in International Journal of Biological Macromolecules. 2019;..
Gligorijević, Nikola, Minić, Simeon L., Robajac, Dragana B., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124" in International Journal of Biological Macromolecules (2019).

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2142
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
UR  - Kon_3473
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005",
url = "Kon_3473"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O.. (2018). Structural changes of fibrinogen as a consequence of cirrhosis. in Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Kon_3473
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. in Thrombosis Research. 2018;166:43-49.
doi:10.1016/j.thromres.2018.04.005
Kon_3473 .
Gligorijević, Nikola, Minić, Simeon L., Krizakova, Martina, Katrlik, Jaroslav, Nedić, Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" in Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .,
Kon_3473 .
4
4
4

Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju

Gligorijević, Nikola

(Универзитет у Београду, Хемијски факултет, 2018)

TY  - THES
AU  - Gligorijević, Nikola
PY  - 2018
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=6386
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:19076/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=50770447
UR  - http://nardus.mpn.gov.rs/123456789/10480
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3162
AB  - Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu...
AB  - Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju
ER  - 
@phdthesis{
author = "Gligorijević, Nikola",
year = "2018",
abstract = "Fibrinogen je vaţan protein primarne i glavni protein sekundarne hemostaze. Nakon povrede, on se dejstvom trombina pretvara u nerastvorni fibrin koji se dalje umreţava, pri čemu nastaje fibrinska mreţa koja ojačava krvni ugrušak na mestu povrede. Da bi fibrinogen obavljao svoju biohemijsku ulogu, bitni su odreĎeni faktori, u koje spadaju njegove posttranslacione modifikacije i interakcije sa drugim proteinima. Posttranslacione modifikacije fibrinogena utiču na njegovu strukturu, strukturu fibrina i interakcije sa drugim proteinima. Fibrin nije pasivna mreţa koja samo daje potporu krvnom ugrušku, već je aktivna struktura koja reguliše svoju sintezu i razgradnju interakcijom sa brojnim proteinima. Zato je vaţno otkriti nove proteine koji sa njim interaguju, a koji imaju uticaj na proces zarastanja povreda.U okviru ove diseretacije, optimizovana je procedura za izolovanje i analizu fibrinogena. Upotrebom dvostrukog taloţenja etanolom dobijen je visoko prečišćen fibrinogen, pogodan za dalju karakterizaciju.Kako je poznato da fibrinogen interaguje sa IGFBP-3 proteinom, postavilo se pitanje da li još neki protein iz grupe vezujućih proteina za IGF, pri fiziološkim uslovima, ima tu sposobnost. Upotrebom većeg broja afinitetnih metoda je pokazano da IGFBP-1 interaguje sa fibrinogenom i da je to opšta fiziološka pojava. Značaj ove interakcije treba sagledavati imajući u vidu da i IGFBP-1 podstiče zarastanje tkivnih povreda, samostalno i kao transporter IGF molekula.Brojne patologije pri kojima se javljaju i koagulopatije, kao što su dijabetes melitus tipa 2 i ciroza jetre, karakteriše izmenjena koncentracija i struktura fibrinogena, što za posledicu ima stvaranje abnormalnog, trombogenog fibrina. Detaljno izučavanje pojedinačnih proteina uključenih u koagulopatiju moţe dati bliţu sliku mehanizma odgovornog za ovu pojavu. Sa druge strane, promene na nivou posttranslacionih modifikacija i strukture fibrinogena sa starenjem mogu doprineti boljem razumevanju prisustva ili odsustva odreĎenih patologija kod starijih ljudi.Struktura fibrinogena sa starenjem se menja. Primenom lektinskog eseja uočeno je povećanje visoko-manoznih i/ili hibridnih N-glikana, tri-/tertaantenarnih kompleksnih glikana sa većim sadrţajem Gal i GlcNAc. Spektrofluorimetrijska analiza je pokazala da kod zdravih ljudi preko 60 godina starosti, fibrinogen ima kompaktniju tercijarnustrukturu..., Fibrinogen is an important protein of primary and main protein of secondary hemostasis. Upon injury, fibrinogen is converted to insoluble fibrin by the action of thrombin. Fibrin further cross-links and creates fibrin network which reinforces blood clotting at the site of injury. There is a significant contribution of posttranslational modifications as well as interactions with other proteins necessary for fulfillment of fibrinogen biochemical role. Posttranslational modifications of fibrinogen influence its structure, fibrin structure and interactions with other proteins. Fibrin is not only a passive network that supports blood clot, but also an active structure that regulates its synthesis and degradation by interacting with many different proteins. For this reason, it is important to identify new proteins which interact with fibrinogen and may also have a role in wound healing.The procedure for isolation and analysis of fibrinogen was optimized in this dissertation. Application of double precipitation using ethanol resulted in highly purified fibrinogen, suitable for further characterisation.Since it is known that fibrinogen interacts with IGFBP-3 protein, the question was raised weather some other protein from the family of the IGF-binding proteins has this ability under physiological conditions. By using several affinity methods, it was shown that IGFBP-1 interacts with fibrinogen and this is a general physiological event. The significance of this interaction should be evaluated taking into consideration that IGFBP-1 itself may have beneficial effect on tissue wound healing, alone and as a transporter of the IGF molecule.Several pathologies accompanied by coagulopathies, such as diabetes mellitus type 2 and cirrhosis, are characterised by altered concentration and structure of fibrinogen, which in turn creates abnormal, thrombogenic fibrin. Detailed study of individual proteins included in coagulopathy may enable closer look at mechanisms responsible for this outcome. On the other hand, changes in posttranslational modifications and structure of fibrinogen with aging may lead to better understanding of presence or absence of certain pathologies associated with ageing.The structure of fibrinogen alteres with aging. An increase of high-mannose and/or hybrid N-glycans, tri-/tetraantennary complex glycans with greater amounts ofGal and GlcNAc was detected by lectin array...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju"
}
Gligorijević, N.. (2018). Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju. in Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Gligorijević N. Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju. in Универзитет у Београду. 2018;..
Gligorijević, Nikola, "Uticaj posttranslacionih modifikacija fibrinogena na njegovu reaktivnost i funkciju" in Универзитет у Београду (2018).

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3265
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
UR  - Kon_3473
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005",
url = "Kon_3473"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O.. (2018). Structural changes of fibrinogen as a consequence of cirrhosis. in Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Kon_3473
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. in Thrombosis Research. 2018;166:43-49.
doi:10.1016/j.thromres.2018.04.005
Kon_3473 .
Gligorijević, Nikola, Minić, Simeon L., Krizakova, Martina, Katrlik, Jaroslav, Nedić, Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" in Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .,
Kon_3473 .
4
4
4

A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia

Gligorijević, Nikola; Stevanović, Nikola R.; Lončar, Nikola L.; Baošić, Rada; Vujčić, Zoran; Božić, Nataša

(Serbian Chemical Soc, Belgrade, 2014)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stevanović, Nikola R.
AU  - Lončar, Nikola L.
AU  - Baošić, Rada
AU  - Vujčić, Zoran
AU  - Božić, Nataša
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1771
AB  - Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia
VL  - 79
IS  - 4
SP  - 411
EP  - 420
DO  - 10.2298/JSC130909155G
UR  - Kon_2654
ER  - 
@article{
author = "Gligorijević, Nikola and Stevanović, Nikola R. and Lončar, Nikola L. and Baošić, Rada and Vujčić, Zoran and Božić, Nataša",
year = "2014",
abstract = "Several natural isolates of Bacillus strains namely 5B, 12B, 16B, 18 and 24B were grown at two different temperatures in submerged fermentation for the production of raw-starch-digesting alpha-amylases. All strains except Bacillus sp. 18 produced more alpha-amylase at 37 degrees C. The hydrolysis of raw cornstarch followed the same pattern. Efficient hydrolysis was obtained with alpha-amylases from Bacillus sp. 5B, 12B, 16B and 24B grown at 37 degrees C and Bacillus sp. 18 grown at 50 degrees C. Zymography after isoelectric focusing showed that alpha-amylases were produced in multiple forms, from 2 to 6, depending on the strain when they were growing at 37 degrees C, while growth at 50 degrees C induced only 1 or 2 isoforms. Thin layer chromatography (TLC) analysis of the hydrolysis products of raw corn and soluble starch by alpha-amylases revealed the production of various mixtures of oligosaccharides. In most cases, G3 was the most dominant product from soluble starch while G2, G3 and G5 were the main products of raw starch hydrolysis. This indicates that the obtained alpha-amylases could be used for starch liquidification or short-chain-oligosaccharide formation, depending on the type of starch (raw or soluble) used for the hydrolysis.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia",
volume = "79",
number = "4",
pages = "411-420",
doi = "10.2298/JSC130909155G",
url = "Kon_2654"
}
Gligorijević, N., Stevanović, N. R., Lončar, N. L., Baošić, R., Vujčić, Z.,& Božić, N.. (2014). A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 79(4), 411-420.
https://doi.org/10.2298/JSC130909155G
Kon_2654
Gligorijević N, Stevanović NR, Lončar NL, Baošić R, Vujčić Z, Božić N. A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia. in Journal of the Serbian Chemical Society. 2014;79(4):411-420.
doi:10.2298/JSC130909155G
Kon_2654 .
Gligorijević, Nikola, Stevanović, Nikola R., Lončar, Nikola L., Baošić, Rada, Vujčić, Zoran, Božić, Nataša, "A thin layer chromatographic comparison of raw and soluble starch hydrolysis patterns of some alpha-amylases from Bacillus sp isolated in Serbia" in Journal of the Serbian Chemical Society, 79, no. 4 (2014):411-420,
https://doi.org/10.2298/JSC130909155G .,
Kon_2654 .
2
2
2

Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia

Lončar, Nikola L.; Gligorijević, Nikola; Božić, Nataša; Vujčić, Zoran

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Gligorijević, Nikola
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1791
AB  - Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - International Biodeterioration and Biodegradation
T1  - Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia
VL  - 91
SP  - 18
EP  - 23
DO  - 10.1016/j.ibiod.2014.03.008
UR  - Kon_2674
ER  - 
@article{
author = "Lončar, Nikola L. and Gligorijević, Nikola and Božić, Nataša and Vujčić, Zoran",
year = "2014",
abstract = "Halotolerant strains of Bacillus amyloliquefaciens were isolated from salt spring in Ovca spa located in Republic of Serbia. Strains exhibit robust spore laccase with high temperature optimum of 65 degrees C while pH optimum is wide and substrate dependant. Ability to oxidize azo dyes was demonstrated. Under optimized conditions more than 85% removal of Congo red dye was achieved at pH 5.7. Substantial resistance to inhibition by high concentration of chloride ions was observed and tolerance of some commonly used cosolvents shows that applicability of these laccases goes beyond decolorization of textile effluents. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "International Biodeterioration and Biodegradation",
title = "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia",
volume = "91",
pages = "18-23",
doi = "10.1016/j.ibiod.2014.03.008",
url = "Kon_2674"
}
Lončar, N. L., Gligorijević, N., Božić, N.,& Vujčić, Z.. (2014). Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation
Elsevier Sci Ltd, Oxford., 91, 18-23.
https://doi.org/10.1016/j.ibiod.2014.03.008
Kon_2674
Lončar NL, Gligorijević N, Božić N, Vujčić Z. Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia. in International Biodeterioration and Biodegradation. 2014;91:18-23.
doi:10.1016/j.ibiod.2014.03.008
Kon_2674 .
Lončar, Nikola L., Gligorijević, Nikola, Božić, Nataša, Vujčić, Zoran, "Congo red degrading laccases from Bacillus amyloliquefaciens strains isolated from salt spring in Serbia" in International Biodeterioration and Biodegradation, 91 (2014):18-23,
https://doi.org/10.1016/j.ibiod.2014.03.008 .,
Kon_2674 .
16
18
22

Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor

Gligorijević, Nikola; Aranđelović, Sandra; Filipović, Lana; Krivokuca, A.; Jankovic, R.; Radulović, Siniša; Ivanović, I.; Grgurić-Šipka, Sanja; Tešić, Živoslav Lj.

(Oxford Univ Press, Oxford, 2012)

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Aranđelović, Sandra
AU  - Filipović, Lana
AU  - Krivokuca, A.
AU  - Jankovic, R.
AU  - Radulović, Siniša
AU  - Ivanović, I.
AU  - Grgurić-Šipka, Sanja
AU  - Tešić, Živoslav Lj.
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1296
PB  - Oxford Univ Press, Oxford
C3  - Annals of Oncology
T1  - Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor
VL  - 23
SP  - 30
EP  - 31
UR  - Kon_2319
ER  - 
@conference{
author = "Gligorijević, Nikola and Aranđelović, Sandra and Filipović, Lana and Krivokuca, A. and Jankovic, R. and Radulović, Siniša and Ivanović, I. and Grgurić-Šipka, Sanja and Tešić, Živoslav Lj.",
year = "2012",
publisher = "Oxford Univ Press, Oxford",
journal = "Annals of Oncology",
title = "Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor",
volume = "23",
pages = "30-31",
url = "Kon_2319"
}
Gligorijević, N., Aranđelović, S., Filipović, L., Krivokuca, A., Jankovic, R., Radulović, S., Ivanović, I., Grgurić-Šipka, S.,& Tešić, Ž. Lj.. (2012). Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor. in Annals of Oncology
Oxford Univ Press, Oxford., 23, 30-31.
Kon_2319
Gligorijević N, Aranđelović S, Filipović L, Krivokuca A, Jankovic R, Radulović S, Ivanović I, Grgurić-Šipka S, Tešić ŽL. Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor. in Annals of Oncology. 2012;23:30-31.
Kon_2319 .
Gligorijević, Nikola, Aranđelović, Sandra, Filipović, Lana, Krivokuca, A., Jankovic, R., Radulović, Siniša, Ivanović, I., Grgurić-Šipka, Sanja, Tešić, Živoslav Lj., "Sensitivity of Human Melanoma Cells on the Activity of Picolinate Ruthenium(Ii)-P-Cymene Complex Alone Or in Combination with Parp Inhibitor" in Annals of Oncology, 23 (2012):30-31,
Kon_2319 .