TY  - JOUR
AU  - Mijin, Nemanja D.
AU  - Milošević, Jelica
AU  - Filipović, Nenad R.
AU  - Mitić, Dragana
AU  - Anđelković, Katarina
AU  - Polović, Natalija Đ.
AU  - Todorović, Tamara R.
PY  - 2022
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/6237
AB  - Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer cell lines were investigated. However, the results of the cytotoxic activity did not correlate with the hydrophobic character of the complexes. To gain further insight into the structure–activity relationship, essential for the design of novel potential drugs, other factors, such as non-specific interactions with cellular proteins, have to be taken into account. To explore the potential non-specific influence of the complexes on protein structures, ovalbumin (OVA) was chosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold. Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effect on OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water may be related to a potential crosslinking that leads to OVA aggregation. © 2022 Serbian Chemical Society. All rights reserved.
T2  - Journal of the Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure
EP  - 1156
IS  - 10
SP  - 1143
VL  - 87
DO  - 10.2298/JSC220518050M
ER  - 

@article{
author = "Mijin, Nemanja D. and Milošević, Jelica and Filipović, Nenad R. and Mitić, Dragana and Anđelković, Katarina and Polović, Natalija Đ. and Todorović, Tamara R.",
year = "2022",
abstract = "Previously, the cytotoxic actions of five Pd(II) complexes with bidentate N-heteroaromatic chelators (complexes 1–5) on a palette of several cancer cell lines were investigated. However, the results of the cytotoxic activity did not correlate with the hydrophobic character of the complexes. To gain further insight into the structure–activity relationship, essential for the design of novel potential drugs, other factors, such as non-specific interactions with cellular proteins, have to be taken into account. To explore the potential non-specific influence of the complexes on protein structures, ovalbumin (OVA) was chosen as a model system to mimic cellular non-specific crowding environments with high protein concentrations. A Fourier-transform infrared spectroscopy study implied that the binding of 3 and 4 led to only moderate alternations in the secondary structures of the protein, without the possibility to penetrate into hydrophobic core of the protein and disruption of protein native fold. Contrary, the effect of complex 5 on OVA secondary structures was concentration-dependent. While the lower concentration of complex 5 had no effect on OVA structure, a doubled concentration of complex 5 led to complete disruption of the content native-like secondary structures. The concentration-dependent effect of complex 5 on the changes in secondary structures and considerable increase in the exposure of OVA hydrophobic surfaces to water may be related to a potential crosslinking that leads to OVA aggregation. © 2022 Serbian Chemical Society. All rights reserved.",
journal = "Journal of the Serbian Chemical Society, Journal of the Serbian Chemical Society",
title = "The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure",
pages = "1156-1143",
number = "10",
volume = "87",
doi = "10.2298/JSC220518050M"
}

Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K., Polović, N. Đ.,& Todorović, T. R.. (2022). The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. in Journal of the Serbian Chemical Society, 87(10), 1143-1156.
https://doi.org/10.2298/JSC220518050M

Mijin ND, Milošević J, Filipović NR, Mitić D, Anđelković K, Polović NĐ, Todorović TR. The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure. in Journal of the Serbian Chemical Society. 2022;87(10):1143-1156.
doi:10.2298/JSC220518050M .

Mijin, Nemanja D., Milošević, Jelica, Filipović, Nenad R., Mitić, Dragana, Anđelković, Katarina, Polović, Natalija Đ., Todorović, Tamara R., "The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure" in Journal of the Serbian Chemical Society, 87, no. 10 (2022):1143-1156,
https://doi.org/10.2298/JSC220518050M . .

TY  - JOUR
AU  - Vatić, Sasa
AU  - Mirković, Nemanja
AU  - Milošević, Jelica R.
AU  - Jovcić, Branko
AU  - Polović, Natalija
PY  - 2020
UR  - http://aspace.agrif.bg.ac.rs/handle/123456789/5296
AB  - Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of 'foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocyto genes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.
PB  - Elsevier, Amsterdam
T2  - International Journal of Food Microbiology
T1  - Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes
VL  - 334
DO  - 10.1016/j.ijfoodmicro.2020.108851
ER  - 

@article{
author = "Vatić, Sasa and Mirković, Nemanja and Milošević, Jelica R. and Jovcić, Branko and Polović, Natalija",
year = "2020",
abstract = "Numerous applications of proteolytic enzymes include dissociation of fermented meat products for the enumeration of 'foodborne pathogenic bacteria. The use of trypsin for this cause is abandoned due to the high concentration of the enzyme affecting released bacteria. Papain, as a suggested replacement, and fig latex preparation with high extent of papain-like enzymes have the potential to be applied for bacteria enumeration. Both enzymatic preparations, originating from papaya and fig, showed a broader range of substrate specificities including gelatinolytic activity, especially prominent in the case of ficin and attributed to both, cysteine protease ficin and serine protease by the analysis of 2D zymography with specific inhibitors. The activity towards native collagen, mild in the case of papain, and extensive in the case of fig latex was proved by structural analysis of digested collagen by infrared spectroscopy. Further exploration of their potential for dissociation of fermented meat products showed that both papain and fig latex enzymes are stable in the presence of detergents Tween 20 and Triton X-100 and effective in the enumeration of Listeria monocytogenes. Gelatenolytic activity, and at least partial collagenolytic activity and stability in procedure conditions make papaya and fig latex proteases potent for this application in significantly lower concentrations than previously used enzymes. As a mixture of proteolytic enzymes with divergent characteristics, fig latex preparation shows higher efficiency in Listeria monocyto genes release than papain, conserved even in the presence of stronger non-ionic detergent Triton X-100.",
publisher = "Elsevier, Amsterdam",
journal = "International Journal of Food Microbiology",
title = "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes",
volume = "334",
doi = "10.1016/j.ijfoodmicro.2020.108851"
}

Vatić, S., Mirković, N., Milošević, J. R., Jovcić, B.,& Polović, N.. (2020). Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology
Elsevier, Amsterdam., 334.
https://doi.org/10.1016/j.ijfoodmicro.2020.108851

Vatić S, Mirković N, Milošević JR, Jovcić B, Polović N. Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes. in International Journal of Food Microbiology. 2020;334.
doi:10.1016/j.ijfoodmicro.2020.108851 .

Vatić, Sasa, Mirković, Nemanja, Milošević, Jelica R., Jovcić, Branko, Polović, Natalija, "Broad range of substrate specificities in papain and fig latex enzymes preparations improve enumeration of Listeria monocytogenes" in International Journal of Food Microbiology, 334 (2020),
https://doi.org/10.1016/j.ijfoodmicro.2020.108851 . .