TY  - JOUR
AU  - Mijin, Nemanja
AU  - Milošević, Jelica
AU  - Stevanović, Sanja
AU  - Petrović, Predrag
AU  - Lolić, Aleksandar
AU  - Urbic, Tomaz
AU  - Polović, Natalija
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7189
AB  - The aggregation of proteins into fibrillar, amyloid-like aggregates generally results in an improved, positive effect on various techno-functional properties within food products, such as gelation, emulsification, and foam stabilization. These highly stable structures, characterized by their repetitive, β-sheet rich motifs, may develop as the result of the thermal treatment of protein-rich food products. Heavy metal ions can influence amyloid-like aggregation of food proteins. Lead(II) and cadmium(II) represent some of the most abundant and common environmental water and food pollutants. In this work, the influence of heavy metal ions, lead and cadmium on amyloid-like aggregation of ovalbumin at high temperatures (90 °C) and under acidic conditions (pH 2.0) was investigated. Ovalbumin is used as a general model for how heavy metals can affect amyloid-like aggregation of a food protein. Structural changes were monitored via Thioflavin T and 8-Anilino-1-naphthalenesulfonic acid fluorescence, Fourier-Transform infrared spectroscopy, atomic force microscopy, dynamic light scattering, as well as computational analyses. The obtained results indicate that the added heavy metal ions bind to different sites within ovalbumin prior to thermal treatment. Lead binding sites are closer to the hydrophobic regions of an protein, while cadmium ion binding sites are more exposed. This specific binding of metal ions affects the morphologies of amyloid-like aggregates, resulting in lead-induced branching of amyloid-like fibrils, or cadmium-induced tangling of fibrils into dense amyloid clusters. This additive effect of heavy metal ions is most evident in ovalbumin samples which contain a mixture of both heavy metal ions.
PB  - Elsevier B.V.
T2  - Food Hydrocolloids
T1  - Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin
VL  - 136
SP  - 108292
DO  - 10.1016/j.foodhyd.2022.108292
ER  - 

@article{
author = "Mijin, Nemanja and Milošević, Jelica and Stevanović, Sanja and Petrović, Predrag and Lolić, Aleksandar and Urbic, Tomaz and Polović, Natalija",
year = "2023",
abstract = "The aggregation of proteins into fibrillar, amyloid-like aggregates generally results in an improved, positive effect on various techno-functional properties within food products, such as gelation, emulsification, and foam stabilization. These highly stable structures, characterized by their repetitive, β-sheet rich motifs, may develop as the result of the thermal treatment of protein-rich food products. Heavy metal ions can influence amyloid-like aggregation of food proteins. Lead(II) and cadmium(II) represent some of the most abundant and common environmental water and food pollutants. In this work, the influence of heavy metal ions, lead and cadmium on amyloid-like aggregation of ovalbumin at high temperatures (90 °C) and under acidic conditions (pH 2.0) was investigated. Ovalbumin is used as a general model for how heavy metals can affect amyloid-like aggregation of a food protein. Structural changes were monitored via Thioflavin T and 8-Anilino-1-naphthalenesulfonic acid fluorescence, Fourier-Transform infrared spectroscopy, atomic force microscopy, dynamic light scattering, as well as computational analyses. The obtained results indicate that the added heavy metal ions bind to different sites within ovalbumin prior to thermal treatment. Lead binding sites are closer to the hydrophobic regions of an protein, while cadmium ion binding sites are more exposed. This specific binding of metal ions affects the morphologies of amyloid-like aggregates, resulting in lead-induced branching of amyloid-like fibrils, or cadmium-induced tangling of fibrils into dense amyloid clusters. This additive effect of heavy metal ions is most evident in ovalbumin samples which contain a mixture of both heavy metal ions.",
publisher = "Elsevier B.V.",
journal = "Food Hydrocolloids",
title = "Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin",
volume = "136",
pages = "108292",
doi = "10.1016/j.foodhyd.2022.108292"
}

Mijin, N., Milošević, J., Stevanović, S., Petrović, P., Lolić, A., Urbic, T.,& Polović, N.. (2023). Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin. in Food Hydrocolloids
Elsevier B.V.., 136, 108292.
https://doi.org/10.1016/j.foodhyd.2022.108292

Mijin N, Milošević J, Stevanović S, Petrović P, Lolić A, Urbic T, Polović N. Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin. in Food Hydrocolloids. 2023;136:108292.
doi:10.1016/j.foodhyd.2022.108292 .

Mijin, Nemanja, Milošević, Jelica, Stevanović, Sanja, Petrović, Predrag, Lolić, Aleksandar, Urbic, Tomaz, Polović, Natalija, "Amyloid-like aggregation influenced by lead(II) and cadmium(II) ions in hen egg white ovalbumin" in Food Hydrocolloids, 136 (2023):108292,
https://doi.org/10.1016/j.foodhyd.2022.108292 . .

TY  - CONF
AU  - Milošević, Jelica
AU  - Mijin, Nemanja
AU  - Maleš, Luka
AU  - Margetić, Aleksandra
AU  - Jovčić, Branko
AU  - Polović, Natalija
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5817
AB  - Proteins are prone to structural changes due to their marginal stability. There are multiple
pathways of structural rearrangements leading to misfolding and aggregation among which
amyloids stand out as highly ordered and remarkably stable forms which appear to be a
global minimum of protein free energy landscape of all proteins. In vitro studies on
different proteins show that destabilizing conditions that favor the state of molten globule
are likely to lead to ordered fibril formation. The presence of various organic and inorganic
molecules was reported to affect amyloid fibril formation, eighter as stimulators or
inhibitors. We investigated the formation of amyloid fibrils of human serum albumin,
ovalbumin and papain in the presence of metal ions, as well as low-molecular-weight
compounds. Proteins were incubated in destabilizing conditions optimized to prolong the
solubility of molten globule state and induce amyloid-like structural changes. The effects
of inorganic and organic additives on fibrillation process were monitored using Thioflavin
T fluorescence, 8-Anilinonaphthalene-1-sulfonic acid fluorescence, Attenuated total
reflection Fourier-transform infrared spectroscopy, electrophoretic and microscopy
techniques. Our results show that the kinetics of amyloid formation is dependent on the
presence of iron, copper, zinc and aluminum salts, as well as different lipophilic lowmolecular-
weight compounds. While some compounds act as complete inhibitors of
fibrillation, others increase the rate of fibrillation process and promote the formation of
mature fibrils.
PB  - University of Belgrade - Falulty of chemistry
PB  - Serbian Biochemical Society
C3  - Proceedings - IX Conference of Serbian Biochemical Society “Diversity in Biochemistry”, 14-16.11.2019. Belgrade, Serbia
T1  - Kinetics of amyloid fibril formation in the presence of metal ions and low-molecular-weight compounds
SP  - 133
UR  - https://hdl.handle.net/21.15107/rcub_cer_5817
ER  - 

@conference{
author = "Milošević, Jelica and Mijin, Nemanja and Maleš, Luka and Margetić, Aleksandra and Jovčić, Branko and Polović, Natalija",
year = "2019",
abstract = "Proteins are prone to structural changes due to their marginal stability. There are multiple
pathways of structural rearrangements leading to misfolding and aggregation among which
amyloids stand out as highly ordered and remarkably stable forms which appear to be a
global minimum of protein free energy landscape of all proteins. In vitro studies on
different proteins show that destabilizing conditions that favor the state of molten globule
are likely to lead to ordered fibril formation. The presence of various organic and inorganic
molecules was reported to affect amyloid fibril formation, eighter as stimulators or
inhibitors. We investigated the formation of amyloid fibrils of human serum albumin,
ovalbumin and papain in the presence of metal ions, as well as low-molecular-weight
compounds. Proteins were incubated in destabilizing conditions optimized to prolong the
solubility of molten globule state and induce amyloid-like structural changes. The effects
of inorganic and organic additives on fibrillation process were monitored using Thioflavin
T fluorescence, 8-Anilinonaphthalene-1-sulfonic acid fluorescence, Attenuated total
reflection Fourier-transform infrared spectroscopy, electrophoretic and microscopy
techniques. Our results show that the kinetics of amyloid formation is dependent on the
presence of iron, copper, zinc and aluminum salts, as well as different lipophilic lowmolecular-
weight compounds. While some compounds act as complete inhibitors of
fibrillation, others increase the rate of fibrillation process and promote the formation of
mature fibrils.",
publisher = "University of Belgrade - Falulty of chemistry, Serbian Biochemical Society",
journal = "Proceedings - IX Conference of Serbian Biochemical Society “Diversity in Biochemistry”, 14-16.11.2019. Belgrade, Serbia",
title = "Kinetics of amyloid fibril formation in the presence of metal ions and low-molecular-weight compounds",
pages = "133",
url = "https://hdl.handle.net/21.15107/rcub_cer_5817"
}

Milošević, J., Mijin, N., Maleš, L., Margetić, A., Jovčić, B.,& Polović, N.. (2019). Kinetics of amyloid fibril formation in the presence of metal ions and low-molecular-weight compounds. in Proceedings - IX Conference of Serbian Biochemical Society “Diversity in Biochemistry”, 14-16.11.2019. Belgrade, Serbia
University of Belgrade - Falulty of chemistry., 133.
https://hdl.handle.net/21.15107/rcub_cer_5817

Milošević J, Mijin N, Maleš L, Margetić A, Jovčić B, Polović N. Kinetics of amyloid fibril formation in the presence of metal ions and low-molecular-weight compounds. in Proceedings - IX Conference of Serbian Biochemical Society “Diversity in Biochemistry”, 14-16.11.2019. Belgrade, Serbia. 2019;:133.
https://hdl.handle.net/21.15107/rcub_cer_5817 .

Milošević, Jelica, Mijin, Nemanja, Maleš, Luka, Margetić, Aleksandra, Jovčić, Branko, Polović, Natalija, "Kinetics of amyloid fibril formation in the presence of metal ions and low-molecular-weight compounds" in Proceedings - IX Conference of Serbian Biochemical Society “Diversity in Biochemistry”, 14-16.11.2019. Belgrade, Serbia (2019):133,
https://hdl.handle.net/21.15107/rcub_cer_5817 .