The effect of non-specific binding of Pd(II) complexes with N-heteroaromatic hydrazone ligands on the protein structure
Аутори
Mijin, Nemanja D.Milošević, Jelica
Filipović, Nenad R.
Mitić, Dragana
Anđelković, Katarina K.
Polović, Natalija
Todorović, Tamara
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 protei...n 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.
Кључне речи:
ovalbumin model system / protein aggregation / DMSO effect / ligand hydrophobicityИзвор:
Journal of the Serbian Chemical Society, 2022, 87, 10, 1143-Издавач:
- Serbian Chemical Society
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200288 (Иновациони центар Хемијског факултета у Београду доо) (RS-MESTD-inst-2020-200288)
Напомена:
- Supplementary material: https://cherry.chem.bg.ac.rs/handle/123456789/5707
Повезане информације:
DOI: 10.2298/JSC220518050M
ISSN: 0352-5139
WoS: 00083542340000
Scopus: 2-s2.0-85143236025
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Mijin, Nemanja D. AU - Milošević, Jelica AU - Filipović, Nenad R. AU - Mitić, Dragana AU - Anđelković, Katarina K. AU - Polović, Natalija AU - Todorović, Tamara PY - 2022 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5686 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. PB - 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 VL - 87 IS - 10 SP - 1143 SP - 1156 DO - 10.2298/JSC220518050M ER -
@article{ author = "Mijin, Nemanja D. and Milošević, Jelica and Filipović, Nenad R. and Mitić, Dragana and Anđelković, Katarina K. and Polović, Natalija and Todorović, Tamara", 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.", publisher = "Serbian Chemical Society", journal = "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", volume = "87", number = "10", pages = "1143-1156", doi = "10.2298/JSC220518050M" }
Mijin, N. D., Milošević, J., Filipović, N. R., Mitić, D., Anđelković, K. K., Polović, N.,& Todorović, T.. (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 Serbian Chemical Society., 87(10), 1143. https://doi.org/10.2298/JSC220518050M
Mijin ND, Milošević J, Filipović NR, Mitić D, Anđelković KK, Polović N, Todorović T. 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. doi:10.2298/JSC220518050M .
Mijin, Nemanja D., Milošević, Jelica, Filipović, Nenad R., Mitić, Dragana, Anđelković, Katarina K., Polović, Natalija, Todorović, Tamara, "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, https://doi.org/10.2298/JSC220518050M . .