TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6485
AB  - Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Antioxidants
T1  - Food Antioxidants and Their Interaction with Human Proteins
VL  - 12
IS  - 4
SP  - 815
DO  - 10.3390/antiox12040815
ER  - 

@article{
author = "Nedić, Olgica and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja and Gligorijević, Nikola",
year = "2023",
abstract = "Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Antioxidants",
title = "Food Antioxidants and Their Interaction with Human Proteins",
volume = "12",
number = "4",
pages = "815",
doi = "10.3390/antiox12040815"
}

Nedić, O., Penezić, A., Minić, S., Radomirović, M., Nikolić, M., Ćirković Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
Multidisciplinary Digital Publishing Institute (MDPI)., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T, Gligorijević N. Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants. 2023;12(4):815.
doi:10.3390/antiox12040815 .

Nedić, Olgica, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, Gligorijević, Nikola, "Food Antioxidants and Their Interaction with Human Proteins" in Antioxidants, 12, no. 4 (2023):815,
https://doi.org/10.3390/antiox12040815 . .

TY  - CONF
AU  - Četić, Danilo
AU  - Miljuš, Goran
AU  - Dobrijević, Zorana
AU  - Gligorijević, Nikola
AU  - Vilotić, Aleksandra
AU  - Nedić, Olgica
AU  - Penezić, Ana
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6663
AB  - Human transferrin (Tf) is a bilobal 76 kDa iron-binding glycoprotein present in human
serum. Each lobe has the ability to bind one ferric ion (Fe3+) and a single synergistic
bicarbonate anion. The main role of Tf is to transport Fe3+ ions through the circulation to
cells, via interaction with transferrin receptor (TFR) on the cell surface. Previously
described methods for Tf isolation and purification are either very time-consuming or
provide Tf of lower final purity. Here we describe a fast and simple FPLC method for the
isolation and purification of Tf from human serum. Serum samples were prepared by
precipitation, while protein purification was performed on FPLC system, using an anionexchange
column. Several different buffers at the same pH were tested. Tf purified by this
method was analyzed by Western blot, followed by immunodetection, as well as with
silver staining after SDS PAGE. Its functionality was tested with respect to iron-binding
capacity (ferozzine method) and its ability to interact with TFR by immunofluorescent
staining. The conformation of purified Tf was analyzed by recording intrinsic fluorescent
emmision spectra originating from Trp residues. The method itself is highly reproducible
(intra- and interday), easy to perform (only two steps) and fast (under an hour), yielding
98% to 99% pure Tf with all buffers. Purified Tf was shown to have retained its ironbinding
capacity, as well as the ability to interact with TFR. Purified Tf also retained its
native three-dimensional structure. Described method for the isolation and purification of
Tf is fast, simple and highly reproducible, yielding a functional Tf of high purity in its
native state while offering the flexibility of using different buffer systems. All of these
features make this protocol a method of choice for the isolation and purification of Tf on a
semi-preparative scale.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Simple two-step semi-preparative isolation and purification of transferrin from human serum
SP  - 66
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cer_6663
ER  - 

@conference{
author = "Četić, Danilo and Miljuš, Goran and Dobrijević, Zorana and Gligorijević, Nikola and Vilotić, Aleksandra and Nedić, Olgica and Penezić, Ana",
year = "2023",
abstract = "Human transferrin (Tf) is a bilobal 76 kDa iron-binding glycoprotein present in human
serum. Each lobe has the ability to bind one ferric ion (Fe3+) and a single synergistic
bicarbonate anion. The main role of Tf is to transport Fe3+ ions through the circulation to
cells, via interaction with transferrin receptor (TFR) on the cell surface. Previously
described methods for Tf isolation and purification are either very time-consuming or
provide Tf of lower final purity. Here we describe a fast and simple FPLC method for the
isolation and purification of Tf from human serum. Serum samples were prepared by
precipitation, while protein purification was performed on FPLC system, using an anionexchange
column. Several different buffers at the same pH were tested. Tf purified by this
method was analyzed by Western blot, followed by immunodetection, as well as with
silver staining after SDS PAGE. Its functionality was tested with respect to iron-binding
capacity (ferozzine method) and its ability to interact with TFR by immunofluorescent
staining. The conformation of purified Tf was analyzed by recording intrinsic fluorescent
emmision spectra originating from Trp residues. The method itself is highly reproducible
(intra- and interday), easy to perform (only two steps) and fast (under an hour), yielding
98% to 99% pure Tf with all buffers. Purified Tf was shown to have retained its ironbinding
capacity, as well as the ability to interact with TFR. Purified Tf also retained its
native three-dimensional structure. Described method for the isolation and purification of
Tf is fast, simple and highly reproducible, yielding a functional Tf of high purity in its
native state while offering the flexibility of using different buffer systems. All of these
features make this protocol a method of choice for the isolation and purification of Tf on a
semi-preparative scale.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Simple two-step semi-preparative isolation and purification of transferrin from human serum",
pages = "66-66",
url = "https://hdl.handle.net/21.15107/rcub_cer_6663"
}

Četić, D., Miljuš, G., Dobrijević, Z., Gligorijević, N., Vilotić, A., Nedić, O.,& Penezić, A.. (2023). Simple two-step semi-preparative isolation and purification of transferrin from human serum. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 66-66.
https://hdl.handle.net/21.15107/rcub_cer_6663

Četić D, Miljuš G, Dobrijević Z, Gligorijević N, Vilotić A, Nedić O, Penezić A. Simple two-step semi-preparative isolation and purification of transferrin from human serum. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:66-66.
https://hdl.handle.net/21.15107/rcub_cer_6663 .

Četić, Danilo, Miljuš, Goran, Dobrijević, Zorana, Gligorijević, Nikola, Vilotić, Aleksandra, Nedić, Olgica, Penezić, Ana, "Simple two-step semi-preparative isolation and purification of transferrin from human serum" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):66-66,
https://hdl.handle.net/21.15107/rcub_cer_6663 .

TY  - CONF
AU  - Miljuš, Goran
AU  - Penezić, Ana
AU  - Noe, Dragana
AU  - Dobrijević, Zorana
AU  - Baralić, Marko
AU  - Robajac, Dragana
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Dimitrijević, Ivan
AU  - Barišić, Goran
AU  - Nedić, Olgica
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6664
AB  - Human serum tansferrin (hsTf) is a major circulatory protein crucial for the
transport/metabolism of Fe3+ ions. By sequestering and delivering ferric ions to target
tissues/cells hsTf maintains redox homeostasis. Oxidative stress (OS), one of the hallmarks
of (patho)physiological conditions, alters protein structure and function. The main role of
hsTf hinges on specific interaction with cellular Tf receptor (TfR) while other interactions
contribute to diverse functions. The aim of this study was to profile interacting partners of
hsTf in the samples of serum coming from patients diagnosed with a wide range of
pathological conditions with underlying OS status. Anti-hsTf pull-down samples were
analysed using mass spectrometry. Data went through analysis by appropriate
bioinformatic tools. Results reveal differences in expression of hsTf interacting proteins in
sample groups of patients suffering from kidney insufficiency subjected to dialysis
treatment (peritoneal-PD or hemo-HD) also with patients with gestational diabetes
compared to respective healthy sample groups. Colorectal cancer stage T3 versus T2 stage
shows an inverse distribution of expression profiles in comparison to healthy samples.
Most prominent differences are seen in hsTf interacting partners involved in the
complement and coagulation cascades and cholesterol metabolic pathways, suggesting a
multifaceted role of hsTf in these processes throughout the course of the disease.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress
SP  - 69
EP  - 69
UR  - https://hdl.handle.net/21.15107/rcub_cer_6664
ER  - 

@conference{
author = "Miljuš, Goran and Penezić, Ana and Noe, Dragana and Dobrijević, Zorana and Baralić, Marko and Robajac, Dragana and Šunderić, Miloš and Gligorijević, Nikola and Dimitrijević, Ivan and Barišić, Goran and Nedić, Olgica",
year = "2023",
abstract = "Human serum tansferrin (hsTf) is a major circulatory protein crucial for the
transport/metabolism of Fe3+ ions. By sequestering and delivering ferric ions to target
tissues/cells hsTf maintains redox homeostasis. Oxidative stress (OS), one of the hallmarks
of (patho)physiological conditions, alters protein structure and function. The main role of
hsTf hinges on specific interaction with cellular Tf receptor (TfR) while other interactions
contribute to diverse functions. The aim of this study was to profile interacting partners of
hsTf in the samples of serum coming from patients diagnosed with a wide range of
pathological conditions with underlying OS status. Anti-hsTf pull-down samples were
analysed using mass spectrometry. Data went through analysis by appropriate
bioinformatic tools. Results reveal differences in expression of hsTf interacting proteins in
sample groups of patients suffering from kidney insufficiency subjected to dialysis
treatment (peritoneal-PD or hemo-HD) also with patients with gestational diabetes
compared to respective healthy sample groups. Colorectal cancer stage T3 versus T2 stage
shows an inverse distribution of expression profiles in comparison to healthy samples.
Most prominent differences are seen in hsTf interacting partners involved in the
complement and coagulation cascades and cholesterol metabolic pathways, suggesting a
multifaceted role of hsTf in these processes throughout the course of the disease.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress",
pages = "69-69",
url = "https://hdl.handle.net/21.15107/rcub_cer_6664"
}

Miljuš, G., Penezić, A., Noe, D., Dobrijević, Z., Baralić, M., Robajac, D., Šunderić, M., Gligorijević, N., Dimitrijević, I., Barišić, G.,& Nedić, O.. (2023). Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 69-69.
https://hdl.handle.net/21.15107/rcub_cer_6664

Miljuš G, Penezić A, Noe D, Dobrijević Z, Baralić M, Robajac D, Šunderić M, Gligorijević N, Dimitrijević I, Barišić G, Nedić O. Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:69-69.
https://hdl.handle.net/21.15107/rcub_cer_6664 .

Miljuš, Goran, Penezić, Ana, Noe, Dragana, Dobrijević, Zorana, Baralić, Marko, Robajac, Dragana, Šunderić, Miloš, Gligorijević, Nikola, Dimitrijević, Ivan, Barišić, Goran, Nedić, Olgica, "Proteomic profiling of anti-transferrin pull-down in patients with underlying oxidative stress" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):69-69,
https://hdl.handle.net/21.15107/rcub_cer_6664 .

TY  - JOUR
AU  - Baralić, Marko
AU  - Robajac, Dragana
AU  - Penezić, Ana
AU  - Brković, Voin
AU  - Gligorijević, Nikola
AU  - Bontić, Ana
AU  - Pavlović, Jelena
AU  - Nikolić, Jelena
AU  - Miljuš, Goran
AU  - Dobrijević, Zorana
AU  - Šunderić, Miloš
AU  - Pažitna, Lucija
AU  - Katrlík, Jaroslav
AU  - Nedić, Olgica
AU  - Laušević, Mirjana
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6445
AB  - In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.
PB  - Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Nutrients
T1  - Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19
VL  - 15
IS  - 9
SP  - 2050
DO  - 10.3390/nu15092050
ER  - 

@article{
author = "Baralić, Marko and Robajac, Dragana and Penezić, Ana and Brković, Voin and Gligorijević, Nikola and Bontić, Ana and Pavlović, Jelena and Nikolić, Jelena and Miljuš, Goran and Dobrijević, Zorana and Šunderić, Miloš and Pažitna, Lucija and Katrlík, Jaroslav and Nedić, Olgica and Laušević, Mirjana",
year = "2023",
abstract = "In previous publications, we pointed out the importance of mannosylation of fibrinogen for the development of cardiovascular complications and fucosylation as a predictor of peritoneal membrane dysfunction in patients on peritoneal dialysis (PD). After a follow-up period of 30 months from the onset of the COVID-19 pandemic, we evaluated the significance of 1,25-dihydroxyvitamin D3 (calcitriol) therapy, primary disease, biochemical and hematologic analyzes, and previously performed glycan analysis by lectin-based microarray as predictors of mortality in this patient group. After univariate Cox regression analysis, diabetes mellitus (DM) and calcitriol therapy were found to be potential predictors of mortality. Additional multivariate Cox regression analysis confirmed that only DM was a predictor of mortality. Nevertheless, the use of calcitriol in therapy significantly reduced mortality in this patient group, as shown by the Kaplan–Meier survival curve. The presence of DM as a concomitant disease proved to be a strong predictor of fatal outcome in PD patients infected with SARS-CoV-2. This is the first study to indicate the importance and beneficial effect of calcitriol therapy on survival in PD patients with COVID-19 infection. In addition, this study points to the possibility that adverse thrombogenic events observed in PD patients during the pandemic may be caused by aberrant fibrinogen glycosylation.",
publisher = "Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Nutrients",
title = "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19",
volume = "15",
number = "9",
pages = "2050",
doi = "10.3390/nu15092050"
}

Baralić, M., Robajac, D., Penezić, A., Brković, V., Gligorijević, N., Bontić, A., Pavlović, J., Nikolić, J., Miljuš, G., Dobrijević, Z., Šunderić, M., Pažitna, L., Katrlík, J., Nedić, O.,& Laušević, M.. (2023). Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients
Switzerland : Multidisciplinary Digital Publishing Institute (MDPI)., 15(9), 2050.
https://doi.org/10.3390/nu15092050

Baralić M, Robajac D, Penezić A, Brković V, Gligorijević N, Bontić A, Pavlović J, Nikolić J, Miljuš G, Dobrijević Z, Šunderić M, Pažitna L, Katrlík J, Nedić O, Laušević M. Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19. in Nutrients. 2023;15(9):2050.
doi:10.3390/nu15092050 .

Baralić, Marko, Robajac, Dragana, Penezić, Ana, Brković, Voin, Gligorijević, Nikola, Bontić, Ana, Pavlović, Jelena, Nikolić, Jelena, Miljuš, Goran, Dobrijević, Zorana, Šunderić, Miloš, Pažitna, Lucija, Katrlík, Jaroslav, Nedić, Olgica, Laušević, Mirjana, "Significance of 1,25-Dihydroxyvitamin D3 on Overall Mortality in Peritoneal Dialysis Patients with COVID-19" in Nutrients, 15, no. 9 (2023):2050,
https://doi.org/10.3390/nu15092050 . .

TY  - CONF
AU  - Nedić, Olgica
AU  - Gligorijević, Nikola
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6728
AB  - Our research work was focused on interactions between resveratrol (R) and tibnnogen (I), (dihydro)alpha-lipoic acid (ALA) and fibrinogen or albumin, and phycocyanobilin (PCB) and catalase. Resveratrol is found in grapes and berries, leafy greens are a source of ALA and alga Spirulina is a source of PCB. L-P interactions were investigated by following-up structural changes of proteins and/or ligands using spectrometric methods (spectrofluorimetry, CD, FTIR) and by examining the primary role of individual proteins upon ligand binding.
PB  - Belgrade : University of Belgrade - Faculty of Agriculture
C3  - Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia
T1  - Food antioxidants and their interaction with human proteins
SP  - 13
EP  - 13
UR  - https://hdl.handle.net/21.15107/rcub_cer_6728
ER  - 

@conference{
author = "Nedić, Olgica and Gligorijević, Nikola and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja",
year = "2022",
abstract = "Our research work was focused on interactions between resveratrol (R) and tibnnogen (I), (dihydro)alpha-lipoic acid (ALA) and fibrinogen or albumin, and phycocyanobilin (PCB) and catalase. Resveratrol is found in grapes and berries, leafy greens are a source of ALA and alga Spirulina is a source of PCB. L-P interactions were investigated by following-up structural changes of proteins and/or ligands using spectrometric methods (spectrofluorimetry, CD, FTIR) and by examining the primary role of individual proteins upon ligand binding.",
publisher = "Belgrade : University of Belgrade - Faculty of Agriculture",
journal = "Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia",
title = "Food antioxidants and their interaction with human proteins",
pages = "13-13",
url = "https://hdl.handle.net/21.15107/rcub_cer_6728"
}

Nedić, O., Gligorijević, N., Penezić, A., Minić, S., Radomirović, M., Nikolić, M.,& Ćirković Veličković, T.. (2022). Food antioxidants and their interaction with human proteins. in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia
Belgrade : University of Belgrade - Faculty of Agriculture., 13-13.
https://hdl.handle.net/21.15107/rcub_cer_6728

Nedić O, Gligorijević N, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T. Food antioxidants and their interaction with human proteins. in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia. 2022;:13-13.
https://hdl.handle.net/21.15107/rcub_cer_6728 .

Nedić, Olgica, Gligorijević, Nikola, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, "Food antioxidants and their interaction with human proteins" in Book of abstracts - 1st European Symposium on Phytochemicals in Medicine and Food (1EuSPMF), 7-9 September 2022, Belgrade, Serbia (2022):13-13,
https://hdl.handle.net/21.15107/rcub_cer_6728 .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Minić, Simeon
AU  - Miljuš, Goran
AU  - Nedić, Olgica
AU  - Penezić, Ana
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4763
AB  - The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation.
AB  - У раду су описане карктеристике везивања дихидро-липоинске киселине (DHLA), познатог суплемента у исхрани и антиоксиданса, за албумин из серума људи (HSA). Процес везивања је праћен применом већег броја спектроскопских метода и молекул-
ским моделовањем. HSA везује DHLA умереним афинитетом, 1,00±0,05×104 M-1. Спектроскопски резултати су показали да је везујуће место IIA (Sudlow I) главно место везивања DHLA за HSA. Експериментални, као и резултати молекулског моделовања, су идентификовали електростатичке (сони мостови) и водоничне везе као главне типове
интеракција. Резултати молекулског моделовања су потврдили да и место Sudlow I може везати DHLA, која је у том случају у специфичној конформацији. Симулација молекулске динамике је показала да је формирани комплекс стабилан. Везивање DHLA не
утиче на структуру протеина, али повећава његову термалну стабилност. Везани DHLA не утиче на подложност HSA трипсинској дигестији. Како је DHLA уобичајен суплемент у исхрани, знање о његовим фармакоконетичким и фармакодинамичким особинама је веома важно. Ово испитивање допуњује досадашња знања детаљном анализом интеракције DHLA са HSA, примарним транспортним протеином лекова у циркулацији.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches
T1  - Физичко-хемијска карактеризација интеракције дихидро-липоинске киселине и албумина из серума људи применом мулти-спектроскопских метода и молекулског моделовања
VL  - 86
IS  - 9
SP  - 795
EP  - 807
DO  - 10.2298/JSC210420041G
ER  - 

@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Minić, Simeon and Miljuš, Goran and Nedić, Olgica and Penezić, Ana",
year = "2021",
abstract = "The binding of a popular food supplement and well-known antioxidant, dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised. The binding was monitored by several spectroscopic methods together with the molecular docking approach. HSA was able to bind DHLA with moderate affinity, 1.00±0.05×104 M-1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Both experimental and molecular docking analysis identified electrostatic (salt bridges) and hydrogen bonds as the key interactions involved in DHLA binding to HSA. Molecular docking confirmed that the Sudlow I site could accommodate DHLA and that the ligand is bound to the protein in a specific conformation. The molecular dynamic simulation showed that the formed complex is stable. Binding of DHLA does not affect the structure of the protein, but it thermally stabilises HSA. Bound DHLA had no effect on the susceptibility of HSA to trypsin digestion. Since DHLA is a commonly used food supplement, knowledge of its pharmacokinetics and pharmacodynamic properties in an organism is very important. This study further expands it by providing a detailed analysis of its interaction with HSA, the primary drug transporter in the circulation., У раду су описане карктеристике везивања дихидро-липоинске киселине (DHLA), познатог суплемента у исхрани и антиоксиданса, за албумин из серума људи (HSA). Процес везивања је праћен применом већег броја спектроскопских метода и молекул-
ским моделовањем. HSA везује DHLA умереним афинитетом, 1,00±0,05×104 M-1. Спектроскопски резултати су показали да је везујуће место IIA (Sudlow I) главно место везивања DHLA за HSA. Експериментални, као и резултати молекулског моделовања, су идентификовали електростатичке (сони мостови) и водоничне везе као главне типове
интеракција. Резултати молекулског моделовања су потврдили да и место Sudlow I може везати DHLA, која је у том случају у специфичној конформацији. Симулација молекулске динамике је показала да је формирани комплекс стабилан. Везивање DHLA не
утиче на структуру протеина, али повећава његову термалну стабилност. Везани DHLA не утиче на подложност HSA трипсинској дигестији. Како је DHLA уобичајен суплемент у исхрани, знање о његовим фармакоконетичким и фармакодинамичким особинама је веома важно. Ово испитивање допуњује досадашња знања детаљном анализом интеракције DHLA са HSA, примарним транспортним протеином лекова у циркулацији.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches, Физичко-хемијска карактеризација интеракције дихидро-липоинске киселине и албумина из серума људи применом мулти-спектроскопских метода и молекулског моделовања",
volume = "86",
number = "9",
pages = "795-807",
doi = "10.2298/JSC210420041G"
}

Gligorijević, N., Šukalović, V., Minić, S., Miljuš, G., Nedić, O.,& Penezić, A.. (2021). Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 86(9), 795-807.
https://doi.org/10.2298/JSC210420041G

Gligorijević N, Šukalović V, Minić S, Miljuš G, Nedić O, Penezić A. Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches. in Journal of the Serbian Chemical Society. 2021;86(9):795-807.
doi:10.2298/JSC210420041G .

Gligorijević, Nikola, Šukalović, Vladimir, Minić, Simeon, Miljuš, Goran, Nedić, Olgica, Penezić, Ana, "Physicochemical characterisation of dihydro-alpha-lipoic acid interaction with human serum albumin by multi-spectroscopic and molecular modelling approaches" in Journal of the Serbian Chemical Society, 86, no. 9 (2021):795-807,
https://doi.org/10.2298/JSC210420041G . .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Penezić, Ana
AU  - Nedić, Olgica
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7279
AB  - A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic
acid (DHLA) is a potent, naturally occurring antioxidant that is
found in higher amounts in plants like spinach, broccoli, potatoes,
tomatoes, carrots, beets and rice. DHLA can be consumed
as a food supplement as well, at doses up to 600 mg/day. DHLA
has an inhibitory effect on coagulation as it can reduce concentrations
of some coagulation factors. This study investigated a
direct interaction between DHLA and fibrinogen, the main protein
in coagulation and hemostasis. DHLA binds fibrinogen with
a moderate straight. Calculated constant from spectrofluorimetric
titration for DHLA/fibrinogen complex was 104 M -1. Fibrinogen
stability remains the same with only marginal structural changes
in its secondary structure favouring more ordered molecular
organisation upon DHLA binding, as determined by Fourier transform
infrared spectroscopy. Coagulation assay showed that
fibrinogen with bound DHLA forms fibrin with thicker fibres, as
measured by coagulation assay and is protected from oxidation to
a certain extent. Docking analysis showed that DHLA may bind
fibrinogen in its D regions, which are directly involved in the fibrin
formation. Obtained results support beneficial effects of DHLA
on fibrinogen and consequently on coagulation process, suggesting
that DHLA supplementation may be indicated for persons with
an increased risk of developing thrombotic complications, particularly
those whose fibrin is characterised by increased oxidative
modification and formation of thinner and less porous fibres.
Although further investigation is needed, our results suggest that
DHLA in complex with fibrinogen can be located at the site of
injury where it may exert antioxidant effects.
PB  - Wiley
C3  - FEBS OpenBio
T1  - Dihydro-alpha-lipoic acid binds and protects fibrinogen from oxidation and affects fibrin formation
VL  - 11
IS  - Supplement 1
SP  - 182
EP  - 183
DO  - 10.1002/2211-5463.13205
ER  - 

@conference{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Penezić, Ana and Nedić, Olgica",
year = "2021",
abstract = "A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic
acid (DHLA) is a potent, naturally occurring antioxidant that is
found in higher amounts in plants like spinach, broccoli, potatoes,
tomatoes, carrots, beets and rice. DHLA can be consumed
as a food supplement as well, at doses up to 600 mg/day. DHLA
has an inhibitory effect on coagulation as it can reduce concentrations
of some coagulation factors. This study investigated a
direct interaction between DHLA and fibrinogen, the main protein
in coagulation and hemostasis. DHLA binds fibrinogen with
a moderate straight. Calculated constant from spectrofluorimetric
titration for DHLA/fibrinogen complex was 104 M -1. Fibrinogen
stability remains the same with only marginal structural changes
in its secondary structure favouring more ordered molecular
organisation upon DHLA binding, as determined by Fourier transform
infrared spectroscopy. Coagulation assay showed that
fibrinogen with bound DHLA forms fibrin with thicker fibres, as
measured by coagulation assay and is protected from oxidation to
a certain extent. Docking analysis showed that DHLA may bind
fibrinogen in its D regions, which are directly involved in the fibrin
formation. Obtained results support beneficial effects of DHLA
on fibrinogen and consequently on coagulation process, suggesting
that DHLA supplementation may be indicated for persons with
an increased risk of developing thrombotic complications, particularly
those whose fibrin is characterised by increased oxidative
modification and formation of thinner and less porous fibres.
Although further investigation is needed, our results suggest that
DHLA in complex with fibrinogen can be located at the site of
injury where it may exert antioxidant effects.",
publisher = "Wiley",
journal = "FEBS OpenBio",
title = "Dihydro-alpha-lipoic acid binds and protects fibrinogen from oxidation and affects fibrin formation",
volume = "11",
number = "Supplement 1",
pages = "182-183",
doi = "10.1002/2211-5463.13205"
}

Gligorijević, N., Šukalović, V., Penezić, A.,& Nedić, O.. (2021). Dihydro-alpha-lipoic acid binds and protects fibrinogen from oxidation and affects fibrin formation. in FEBS OpenBio
Wiley., 11(Supplement 1), 182-183.
https://doi.org/10.1002/2211-5463.13205

Gligorijević N, Šukalović V, Penezić A, Nedić O. Dihydro-alpha-lipoic acid binds and protects fibrinogen from oxidation and affects fibrin formation. in FEBS OpenBio. 2021;11(Supplement 1):182-183.
doi:10.1002/2211-5463.13205 .

Gligorijević, Nikola, Šukalović, Vladimir, Penezić, Ana, Nedić, Olgica, "Dihydro-alpha-lipoic acid binds and protects fibrinogen from oxidation and affects fibrin formation" in FEBS OpenBio, 11, no. Supplement 1 (2021):182-183,
https://doi.org/10.1002/2211-5463.13205 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Penezić, Ana
AU  - Nedić, Olgica
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3378
AB  - A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation
VL  - 147
SP  - 319
EP  - 325
DO  - 10.1016/j.ijbiomac.2020.01.098
ER  - 

@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Penezić, Ana and Nedić, Olgica",
year = "2020",
abstract = "A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation",
volume = "147",
pages = "319-325",
doi = "10.1016/j.ijbiomac.2020.01.098"
}

Gligorijević, N., Šukalović, V., Penezić, A.,& Nedić, O.. (2020). Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules
Elsevier., 147, 319-325.
https://doi.org/10.1016/j.ijbiomac.2020.01.098

Gligorijević N, Šukalović V, Penezić A, Nedić O. Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules. 2020;147:319-325.
doi:10.1016/j.ijbiomac.2020.01.098 .

Gligorijević, Nikola, Šukalović, Vladimir, Penezić, Ana, Nedić, Olgica, "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation" in International Journal of Biological Macromolecules, 147 (2020):319-325,
https://doi.org/10.1016/j.ijbiomac.2020.01.098 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Šukalović, Vladimir
AU  - Penezić, Ana
AU  - Nedić, Olgica
PY  - 2020
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3385
AB  - A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.
PB  - Elsevier
T2  - International Journal of Biological Macromolecules
T1  - Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation
VL  - 147
SP  - 319
EP  - 325
DO  - 10.1016/j.ijbiomac.2020.01.098
ER  - 

@article{
author = "Gligorijević, Nikola and Šukalović, Vladimir and Penezić, Ana and Nedić, Olgica",
year = "2020",
abstract = "A reduced form of the alpha-lipoic acid, dihydro-alpha-lipoic acid (DHLA) is a potent, naturally occurring antioxidant which can be consumed as food constituent or as supplement at doses up to 600 mg/day. DHLA has inhibitory effect on coagulation as it can reduce concentrations of some coagulation factors. In this study, a direct interaction between DHLA and fibrinogen, the main protein in coagulation, is described. Binding constant for DHLA/fibrinogen complex is of moderate strength (104) and interaction probably occurs in D regions of fibrinogen, as shown by docking simulations. Fibrinogen stability remains the same with only marginal structural changes in its secondary structure favouring more ordered molecular organisation upon DHLA binding. Fibrinogen with bound DHLA forms fibrin with thicker fibers, as measured by coagulation assay and is protected from oxidation to certain extent. Obtained results support beneficial effects of DHLA on fibrinogen and consequently on coagulation process, suggesting that DHLA supplementation may be indicated for persons with an increased risk of developing thrombotic complications, particularly those whose fibrin is characterised by increased oxidative modification and formation of thinner and less porous fibers. Also, DHLA in complex with fibrinogen can be located at site of injury where it may exert antioxidant effects.",
publisher = "Elsevier",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation",
volume = "147",
pages = "319-325",
doi = "10.1016/j.ijbiomac.2020.01.098"
}

Gligorijević, N., Šukalović, V., Penezić, A.,& Nedić, O.. (2020). Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules
Elsevier., 147, 319-325.
https://doi.org/10.1016/j.ijbiomac.2020.01.098

Gligorijević N, Šukalović V, Penezić A, Nedić O. Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation. in International Journal of Biological Macromolecules. 2020;147:319-325.
doi:10.1016/j.ijbiomac.2020.01.098 .

Gligorijević, Nikola, Šukalović, Vladimir, Penezić, Ana, Nedić, Olgica, "Characterisation of the binding of dihydro-alpha-lipoic acid to fibrinogen and the effects on fibrinogen oxidation and fibrin formation" in International Journal of Biological Macromolecules, 147 (2020):319-325,
https://doi.org/10.1016/j.ijbiomac.2020.01.098 . .