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 .