TY  - JOUR
AU  - Prodić, Ivana
AU  - Krstić Ristivojević, Maja
AU  - Smiljanić, Katarina
PY  - 2023
UR  - https://www.mdpi.com/2076-3921/12/4/886
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1886
AB  - Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.
T2  - Antioxidants
T2  - Antioxidants
T1  - Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies
IS  - 4
SP  - 886
VL  - 12
DO  - 10.3390/antiox12040886
ER  - 

@article{
author = "Prodić, Ivana and Krstić Ristivojević, Maja and Smiljanić, Katarina",
year = "2023",
abstract = "Thermally processed peanuts are ideal plant models for studying the relationship between allergenicity and antioxidant capacity of protein-rich foods, besides lipids, carbohydrates and phytochemicals. Peanut is highly praised in the human diet; however, it is rich in allergens (>75% of total proteins). One-third of peanut allergens belong to the products of genes responsible for the defence of plants against stress conditions. The proximate composition of major peanut macromolecules and polyphenols is reviewed, focusing on the identity and relative abundance of all peanut proteins derived from recent proteomic studies. The importance of thermal processing, gastrointestinal digestion (performed by INFOGEST protocol) and their influence on allergenicity and antioxidant properties of protein-rich plant food matrices is elaborated. Antioxidant properties of bioactive peptides from nuts were also considered. Moreover, there are no studies dealing simultaneously with the antioxidant and allergenic properties of protein- and polyphenol-rich foods, considering all the molecules that can significantly contribute to the antioxidant capacity during and after gastrointestinal digestion. In summary, proteins and carbohydrates are underappreciated sources of antioxidant power released during the gastrointestinal digestion of protein-rich plant foods, and it is crucial to decipher their antioxidant contribution in addition to polyphenols and vitamins before and after gastrointestinal digestion.",
journal = "Antioxidants, Antioxidants",
title = "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies",
number = "4",
pages = "886",
volume = "12",
doi = "10.3390/antiox12040886"
}

Prodić, I., Krstić Ristivojević, M.,& Smiljanić, K.. (2023). Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants, 12(4), 886.
https://doi.org/10.3390/antiox12040886

Prodić I, Krstić Ristivojević M, Smiljanić K. Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies. in Antioxidants. 2023;12(4):886.
doi:10.3390/antiox12040886 .

Prodić, Ivana, Krstić Ristivojević, Maja, Smiljanić, Katarina, "Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion—Peanuts as Our Antioxidant Friend or Foe in Allergies" in Antioxidants, 12, no. 4 (2023):886,
https://doi.org/10.3390/antiox12040886 . .

TY  - CONF
AU  - Pantelić, Ana
AU  - Prodić, Ivana
AU  - Milić, Dejana
AU  - Senćanski, Milan
AU  - Vidović, Marija
PY  - 2023
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2149
AB  - Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period and
fully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, no
specific cellular targets of LEAPs have been identified so far.
Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydrated
and desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterised
and classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.
Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even
17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globular
proteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage and
aggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.
Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.
PB  - Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade
C3  - CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
T1  - Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica
EP  - 110
SP  - 110
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2149
ER  - 

@conference{
author = "Pantelić, Ana and Prodić, Ivana and Milić, Dejana and Senćanski, Milan and Vidović, Marija",
year = "2023",
abstract = "Introduction: Resurrection plants (such as Ramonda serbica) can survive a long desiccation period and
fully resume their metabolism upon watering. The hallmark of desiccation tolerance (DT) is the accumulation of protective, intrinsically disordered proteins(IDPs), called late embryogenesis abundant proteins (LEAPs). Although their high structural plasticity allows them to interact with various partners, no
specific cellular targets of LEAPs have been identified so far.
Methods: To identify LEAPsinvolved in DT, differential transcriptome and proteome analyses of hydrated
and desiccated R. serbica leaves were performed. The identified LEAPs were structurally characterised
and classified. To evaluate theirstructural propertiesin vitro and their potential functionsin vivo, the representative RsLEA proteins, were produced in Escherichia coli using recombinant DNA technology.
Results: Members of the LEA4 protein family represent the majority of desiccation-inducible LEAPs. Even
17 proteins belonging to the LEA4 protein family group were induced by desiccation. They show high disorder propensity (82 %), and at the same time, a high tendency to form α-helices (>80%). Although recombinant DNA technology has traditionally been used to overexpress and purify various globular
proteins, the production of IDPsis challenging due to their high susceptibility to proteolytic cleavage and
aggregation. Nevertheless, the representative LEAPs containing hexa-Histagsimmunoglobulin G-binding protein and a proteolytic TEV site were produced, purified and cleaved by TEV protease.
Conclusion: The combination of in silico and in vitro results will be crucial for the identification of endogenous partners of LEAPs, providing further insight into their role in DT.",
publisher = "Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade",
journal = "CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia",
title = "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica",
pages = "110-110",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2149"
}

Pantelić, A., Prodić, I., Milić, D., Senćanski, M.,& Vidović, M.. (2023). Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia
Institute of Molecular Genetics and Genetic Engineering (IMGGE), University of Belgrade., 110-110.
https://hdl.handle.net/21.15107/rcub_imagine_2149

Pantelić A, Prodić I, Milić D, Senćanski M, Vidović M. Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica. in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia. 2023;:110-110.
https://hdl.handle.net/21.15107/rcub_imagine_2149 .

Pantelić, Ana, Prodić, Ivana, Milić, Dejana, Senćanski, Milan, Vidović, Marija, "Drying without dying: revealing the role of late embryogenesis abundant proteins during desiccation in Ramonda serbica" in CoMBoS2 – the Second Congress of Molecular Biologists of Serbia, Abstract Book – Trends in Molecular Biology, Special issue 06-08 October 2023, Belgrade, Serbia (2023):110-110,
https://hdl.handle.net/21.15107/rcub_imagine_2149 .

TY  - CONF
AU  - Senćanski, Milan
AU  - Prodić, Ivana
AU  - Pantelić, Ana
AU  - Vidović, Marija
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1997
AB  - Drought stress is one of the greatest threats to global food security, posing a major challenge
to agriculture. Understanding the molecular mechanisms underlying desiccation tolerance
in resurrection plants like Ramonda serbica Panc., can provide valuable insights for improving
crop resilience. Dehydrins are intrinsically disordered proteins known to accumulate in these
plants in response to desiccation. Among several proposed physiological roles, it has been
suggested that dehydrins can protect DNA from damage during water shortage. Here, we
have characterised dehydrins from R. serbica, selected a representative one and evaluated
its potential to interact with DNA.
Most of the R. serbica dehydrins were designated as hydrophilins (glycine content >6%;
GRAVY index <1). They exhibit a high disorder propensity, making them quite dynamic
in solution. Furthermore, they were predicted to localize in the nucleus. To examine the
potential interactions with DNA in silico, we have selected a representative, highly hydrophilic
dehydrin (Gravy index: –1.29) containing a high percentage of glycine (22.6%) and charged
amino acids (lysine, glutamate and aspartate). Its 3D structures were determined using the
Phyre 2 intensive modelling and AlphaFold.
The dehydrin-DNA complex was manually adjusted, following molecular dynamic simulation
(MDS) in both cases of hydration and desiccation. To simulate complete hydration, the DNAdehydrin
complex was solvated in a water box, with final dimensions of 100×69×82 Å,
neutralised with 0.15 M NaCl. The system underwent a 10,000-step energy minimization,
consecutive 1250 ps equilibration NVE (constant number of atoms, volume and energy)
heating from 10 K to 298 K and 100 ns NPT (constant number of atoms, pressure and
temperature) MD production at 1 bar, and 1 fs integration step. In all simulations, periodic
boundary conditions (PBC) were implemented and the CHARMM36 force field was used.
The obtained results revealed that selected dehydrin can interact with both minor and major
DNA grooves. The phosphate groups from the DNA molecule form salt bridges with the
positively charged lysines from polylysine, K-segment, contributing to the complex stability.
Overall, we have provided evidence for possible dehydrin-DNA interactions. However, the
exact nature and significance of these interactions is still an area of active research in vitro.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - Dehydrins in the service of protecting the DNA helix from the aspect of molecular dynamics (MD)
EP  - 57
SP  - 57
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1997
ER  - 

@conference{
author = "Senćanski, Milan and Prodić, Ivana and Pantelić, Ana and Vidović, Marija",
year = "2023",
abstract = "Drought stress is one of the greatest threats to global food security, posing a major challenge
to agriculture. Understanding the molecular mechanisms underlying desiccation tolerance
in resurrection plants like Ramonda serbica Panc., can provide valuable insights for improving
crop resilience. Dehydrins are intrinsically disordered proteins known to accumulate in these
plants in response to desiccation. Among several proposed physiological roles, it has been
suggested that dehydrins can protect DNA from damage during water shortage. Here, we
have characterised dehydrins from R. serbica, selected a representative one and evaluated
its potential to interact with DNA.
Most of the R. serbica dehydrins were designated as hydrophilins (glycine content >6%;
GRAVY index <1). They exhibit a high disorder propensity, making them quite dynamic
in solution. Furthermore, they were predicted to localize in the nucleus. To examine the
potential interactions with DNA in silico, we have selected a representative, highly hydrophilic
dehydrin (Gravy index: –1.29) containing a high percentage of glycine (22.6%) and charged
amino acids (lysine, glutamate and aspartate). Its 3D structures were determined using the
Phyre 2 intensive modelling and AlphaFold.
The dehydrin-DNA complex was manually adjusted, following molecular dynamic simulation
(MDS) in both cases of hydration and desiccation. To simulate complete hydration, the DNAdehydrin
complex was solvated in a water box, with final dimensions of 100×69×82 Å,
neutralised with 0.15 M NaCl. The system underwent a 10,000-step energy minimization,
consecutive 1250 ps equilibration NVE (constant number of atoms, volume and energy)
heating from 10 K to 298 K and 100 ns NPT (constant number of atoms, pressure and
temperature) MD production at 1 bar, and 1 fs integration step. In all simulations, periodic
boundary conditions (PBC) were implemented and the CHARMM36 force field was used.
The obtained results revealed that selected dehydrin can interact with both minor and major
DNA grooves. The phosphate groups from the DNA molecule form salt bridges with the
positively charged lysines from polylysine, K-segment, contributing to the complex stability.
Overall, we have provided evidence for possible dehydrin-DNA interactions. However, the
exact nature and significance of these interactions is still an area of active research in vitro.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "Dehydrins in the service of protecting the DNA helix from the aspect of molecular dynamics (MD)",
pages = "57-57",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1997"
}

Senćanski, M., Prodić, I., Pantelić, A.,& Vidović, M.. (2023). Dehydrins in the service of protecting the DNA helix from the aspect of molecular dynamics (MD). in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 57-57.
https://hdl.handle.net/21.15107/rcub_imagine_1997

Senćanski M, Prodić I, Pantelić A, Vidović M. Dehydrins in the service of protecting the DNA helix from the aspect of molecular dynamics (MD). in 4th Belgrade Bioinformatics Conference. 2023;4:57-57.
https://hdl.handle.net/21.15107/rcub_imagine_1997 .

Senćanski, Milan, Prodić, Ivana, Pantelić, Ana, Vidović, Marija, "Dehydrins in the service of protecting the DNA helix from the aspect of molecular dynamics (MD)" in 4th Belgrade Bioinformatics Conference, 4 (2023):57-57,
https://hdl.handle.net/21.15107/rcub_imagine_1997 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Jovanović, Vesna
AU  - Smiljanić, Katarina
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2052
AB  - Porcine-derived trypsin generated proteomic data of the major peanut allergen Ara h 1
from the peanut was reassessed to search for possible facilitating/hindrance effects on
trypsin digestion efficacy caused by post-translational and chemical modifications (PTMs)
positioned on arginine or lysine (K/R) residues. If the potential effects caused by PTMs are
observed with porcine trypsin, they can be just augmented and more pronounced within
human intestinal digestion. The reasoning is in inferior performance of human trypsin
compared to porcine-derived used in proteomic digestion protocols, also in the lower
trypsin-to-sample ratio and much shorter digestion times, even though gastric digestion
precedes and trypsin is not the sole digestive enzyme.
A novel method was developed to decipher cleavage or miscleavage outcomes at scissile
bonds in each, modified and unmodified sequence counterparts, using PEAKS Studio-X+
(Bioinformatics Solutions Inc., Ontario, Canada) in the reassessment of high-resolution
tandem mass spectrometry data, from 18-hour long trypsin digestion proteomic protocols.
In general, eight site-specific and modified K/R residues with methylation, dihydroxy
and formylation showed significantly higher content of miscleaved bonds (at least >10%)
compared to their unmodified counterpart peptides. Specifically, dihydroxylation and
formylation hindered trypsin efficacy, while methylation on several K/R showed opposite
effects.
It is essential to elucidate the specific impacts of modifications on trypsin digestion
performance and if there are additional effects generated by food processing, which could
influence digestion outcomes and allergenicity of food proteins/peptides.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes
EP  - 107
SP  - 107
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2052
ER  - 

@conference{
author = "Prodić, Ivana and Đukić, Teodora and Jovanović, Vesna and Smiljanić, Katarina",
year = "2023",
abstract = "Porcine-derived trypsin generated proteomic data of the major peanut allergen Ara h 1
from the peanut was reassessed to search for possible facilitating/hindrance effects on
trypsin digestion efficacy caused by post-translational and chemical modifications (PTMs)
positioned on arginine or lysine (K/R) residues. If the potential effects caused by PTMs are
observed with porcine trypsin, they can be just augmented and more pronounced within
human intestinal digestion. The reasoning is in inferior performance of human trypsin
compared to porcine-derived used in proteomic digestion protocols, also in the lower
trypsin-to-sample ratio and much shorter digestion times, even though gastric digestion
precedes and trypsin is not the sole digestive enzyme.
A novel method was developed to decipher cleavage or miscleavage outcomes at scissile
bonds in each, modified and unmodified sequence counterparts, using PEAKS Studio-X+
(Bioinformatics Solutions Inc., Ontario, Canada) in the reassessment of high-resolution
tandem mass spectrometry data, from 18-hour long trypsin digestion proteomic protocols.
In general, eight site-specific and modified K/R residues with methylation, dihydroxy
and formylation showed significantly higher content of miscleaved bonds (at least >10%)
compared to their unmodified counterpart peptides. Specifically, dihydroxylation and
formylation hindered trypsin efficacy, while methylation on several K/R showed opposite
effects.
It is essential to elucidate the specific impacts of modifications on trypsin digestion
performance and if there are additional effects generated by food processing, which could
influence digestion outcomes and allergenicity of food proteins/peptides.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes",
pages = "107-107",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2052"
}

Prodić, I., Đukić, T., Jovanović, V.,& Smiljanić, K.. (2023). The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes. in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 107-107.
https://hdl.handle.net/21.15107/rcub_imagine_2052

Prodić I, Đukić T, Jovanović V, Smiljanić K. The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes. in 4th Belgrade Bioinformatics Conference. 2023;4:107-107.
https://hdl.handle.net/21.15107/rcub_imagine_2052 .

Prodić, Ivana, Đukić, Teodora, Jovanović, Vesna, Smiljanić, Katarina, "The use of tryptic food protein digests data in public proteomic repositories to assess the effects of chemical and post-translational modifications on digestion outcomes" in 4th Belgrade Bioinformatics Conference, 4 (2023):107-107,
https://hdl.handle.net/21.15107/rcub_imagine_2052 .

TY  - CONF
AU  - Pantelić, Ana
AU  - Senćanski, Milan
AU  - Prodić, Ivana
AU  - Milić, Dejana
AU  - Vidović, Marija
PY  - 2023
UR  - https://ml4ngp.eu/conference-bratislava/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1934
PB  - European Cooperation in Science and Technology
C3  - Non-globular proteins in the era of machine learning
T1  - Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation
EP  - 6
SP  - 5
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1934
ER  - 

@conference{
author = "Pantelić, Ana and Senćanski, Milan and Prodić, Ivana and Milić, Dejana and Vidović, Marija",
year = "2023",
publisher = "European Cooperation in Science and Technology",
journal = "Non-globular proteins in the era of machine learning",
title = "Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation",
pages = "6-5",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1934"
}

Pantelić, A., Senćanski, M., Prodić, I., Milić, D.,& Vidović, M.. (2023). Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation. in Non-globular proteins in the era of machine learning
European Cooperation in Science and Technology., 5-6.
https://hdl.handle.net/21.15107/rcub_imagine_1934

Pantelić A, Senćanski M, Prodić I, Milić D, Vidović M. Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation. in Non-globular proteins in the era of machine learning. 2023;:5-6.
https://hdl.handle.net/21.15107/rcub_imagine_1934 .

Pantelić, Ana, Senćanski, Milan, Prodić, Ivana, Milić, Dejana, Vidović, Marija, "Group 4 late embryogenesis abundant (LEA) proteins as a model to stydy propensity for oligomerisation" in Non-globular proteins in the era of machine learning (2023):5-6,
https://hdl.handle.net/21.15107/rcub_imagine_1934 .

TY  - CONF
AU  - Vidović, Marija
AU  - Pantelić, Ana
AU  - Senćanski, Milan
AU  - Prodić, Ivana
PY  - 2023
UR  - https://ml4ngp.eu/conference-bratislava/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1933
PB  - European Cooperation in Science and Technology
C3  - Non-globular proteins in the era of machine learning
T1  - LEA4 proteins: How disordered are they?
EP  - 50
SP  - 49
UR  - https://hdl.handle.net/21.15107/rcub_imagine_1933
ER  - 

@conference{
author = "Vidović, Marija and Pantelić, Ana and Senćanski, Milan and Prodić, Ivana",
year = "2023",
publisher = "European Cooperation in Science and Technology",
journal = "Non-globular proteins in the era of machine learning",
title = "LEA4 proteins: How disordered are they?",
pages = "50-49",
url = "https://hdl.handle.net/21.15107/rcub_imagine_1933"
}

Vidović, M., Pantelić, A., Senćanski, M.,& Prodić, I.. (2023). LEA4 proteins: How disordered are they?. in Non-globular proteins in the era of machine learning
European Cooperation in Science and Technology., 49-50.
https://hdl.handle.net/21.15107/rcub_imagine_1933

Vidović M, Pantelić A, Senćanski M, Prodić I. LEA4 proteins: How disordered are they?. in Non-globular proteins in the era of machine learning. 2023;:49-50.
https://hdl.handle.net/21.15107/rcub_imagine_1933 .

Vidović, Marija, Pantelić, Ana, Senćanski, Milan, Prodić, Ivana, "LEA4 proteins: How disordered are they?" in Non-globular proteins in the era of machine learning (2023):49-50,
https://hdl.handle.net/21.15107/rcub_imagine_1933 .

TY  - JOUR
AU  - Perusko, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović, Jelena
AU  - Minić, Simeon
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Cirkovic Velicković, Tanja
PY  - 2017
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1088
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
EP  - 752
SP  - 744
VL  - 232
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 

@article{
author = "Perusko, Marija and Al-Hanish, Ayah and Mihailović, Jelena and Minić, Simeon and Trifunović, Sara and Prodić, Ivana and Cirkovic Velicković, Tanja",
year = "2017",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
pages = "752-744",
volume = "232",
doi = "10.1016/j.foodchem.2017.04.074"
}

Perusko, M., Al-Hanish, A., Mihailović, J., Minić, S., Trifunović, S., Prodić, I.,& Cirkovic Velicković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074

Perusko M, Al-Hanish A, Mihailović J, Minić S, Trifunović S, Prodić I, Cirkovic Velicković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752.
doi:10.1016/j.foodchem.2017.04.074 .

Perusko, Marija, Al-Hanish, Ayah, Mihailović, Jelena, Minić, Simeon, Trifunović, Sara, Prodić, Ivana, Cirkovic Velicković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 . .