Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion
Аутори
Warżajtis, BeataGlišić, Biljana Đ.
Savić, Nada D.
Pavić, Aleksandar
Vojnović, Sandra
Veselinović, Aleksandar
Nikodinović-Runić, Jasmina
Rychlewska, Urszula
Đuran, Miloš I.
Чланак у часопису (Рецензирана верзија)
Метаподаци
Приказ свих података о документуАпстракт
Gold(III) complexes with different L-histidine-containing dipeptides, [Au(Gly-L-His-N-A,N-P,N3)Cl]Cl center dot 3H(2)O (1a), [Au(Gly-L-His-N-A,N-P,N-3)Cl]NO3 center dot 1.25H(2)O (1b), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (2a), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl]NO3 center dot 2.5H(2)O (2b), [Au(L-Val-L-His-N-A,N-P,N-3)Cl]Cl center dot 2H(2)O (3), [Au(L-Leu-L-His-N-A,N-P,N-3)Cl]Cl (4a) and [Au(L-Leu-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (4b), have been synthesized and structurally characterized by spectroscopic (1H NMR, IR and UV-vis) and single-crystal X-ray diffraction techniques. The antimicrobial efficiency of these gold(III) complexes, along with K[AuCl4] and the corresponding dipeptides, was evaluated against the broad panel of Gram-positive and Gram-negative bacteria and fungi, displaying their moderate inhibiting activity. Moreover, the cytotoxic properties of the investigated complexes were assessed against the normal human lung fibroblast cell line (MRC5) and... two human cancer, cervix (HeLa) and lung (A549) cell lines. None of the complexes exerted significant cytotoxic activity; nevertheless complexes that did show selectivity in terms of cancer vs. normal cell lines (2a/b and 4a/b) have been evaluated using zebrafish (Danio rerio) embryos for toxicity and antiangiogenic potential. Although the gold(III) complexes achieved an antiangiogenic effect comparable to the known angiogenic inhibitors auranofin and sunitinib malate at 30-fold higher concentrations, they had no cardiovascular side effects, which commonly accompany auranofin and sunitinib malate treatment. Finally, binding of the gold(III) complexes to the active sites of both human and bacterial (Escherichia coli) thioredoxin reductases (TrxRs) was demonstrated by conducting a molecular docking study, suggesting that the mechanism of biological action of these complexes can be associated with their interaction with the TrxR active site.
Извор:
Dalton Transactions, 2017, 46, 8, 2594-2608Издавач:
- Royal Soc Chemistry, Cambridge
Финансирање / пројекти:
- Синтеза нових комплекса метала и испитивање њихових реакција са пептидима (RS-172036)
- Изучавање микробиолошког диверзитета и карактеризација корисних срединских микроорганизама (RS-173048)
- SupraMedChem'Balkans.Net SCOPES Institutional Partnership [IZ74Z0_160515]
Напомена:
- This is the peer-reviewed version of the following article: Warzajtis, B.; Glišić, B. D.; Savić, N. D.; Pavic, A.; Vojnovic, S.; Veselinović, A.; Nikodinovic-Runic, J.; Rychlewska, U.; Djuran, M. I. Mononuclear Gold(Iii) Complexes with l-Histidine-Containing Dipeptides: Tuning the Structural and Biological Properties by Variation of the N-Terminal Amino Acid and Counter Anion. Dalton Transactions 2017, 46 (8), 2594–2608. https://doi.org/10.1039/c6dt04862e
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3108
DOI: 10.1039/c6dt04862e
ISSN: 1477-9226
WoS: 000395864900022
Scopus: 2-s2.0-85013631334
Колекције
Институција/група
Inovacioni centar / Innovation CentreTY - JOUR AU - Warżajtis, Beata AU - Glišić, Biljana Đ. AU - Savić, Nada D. AU - Pavić, Aleksandar AU - Vojnović, Sandra AU - Veselinović, Aleksandar AU - Nikodinović-Runić, Jasmina AU - Rychlewska, Urszula AU - Đuran, Miloš I. PY - 2017 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3107 AB - Gold(III) complexes with different L-histidine-containing dipeptides, [Au(Gly-L-His-N-A,N-P,N3)Cl]Cl center dot 3H(2)O (1a), [Au(Gly-L-His-N-A,N-P,N-3)Cl]NO3 center dot 1.25H(2)O (1b), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (2a), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl]NO3 center dot 2.5H(2)O (2b), [Au(L-Val-L-His-N-A,N-P,N-3)Cl]Cl center dot 2H(2)O (3), [Au(L-Leu-L-His-N-A,N-P,N-3)Cl]Cl (4a) and [Au(L-Leu-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (4b), have been synthesized and structurally characterized by spectroscopic (1H NMR, IR and UV-vis) and single-crystal X-ray diffraction techniques. The antimicrobial efficiency of these gold(III) complexes, along with K[AuCl4] and the corresponding dipeptides, was evaluated against the broad panel of Gram-positive and Gram-negative bacteria and fungi, displaying their moderate inhibiting activity. Moreover, the cytotoxic properties of the investigated complexes were assessed against the normal human lung fibroblast cell line (MRC5) and two human cancer, cervix (HeLa) and lung (A549) cell lines. None of the complexes exerted significant cytotoxic activity; nevertheless complexes that did show selectivity in terms of cancer vs. normal cell lines (2a/b and 4a/b) have been evaluated using zebrafish (Danio rerio) embryos for toxicity and antiangiogenic potential. Although the gold(III) complexes achieved an antiangiogenic effect comparable to the known angiogenic inhibitors auranofin and sunitinib malate at 30-fold higher concentrations, they had no cardiovascular side effects, which commonly accompany auranofin and sunitinib malate treatment. Finally, binding of the gold(III) complexes to the active sites of both human and bacterial (Escherichia coli) thioredoxin reductases (TrxRs) was demonstrated by conducting a molecular docking study, suggesting that the mechanism of biological action of these complexes can be associated with their interaction with the TrxR active site. PB - Royal Soc Chemistry, Cambridge T2 - Dalton Transactions T1 - Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion VL - 46 IS - 8 SP - 2594 EP - 2608 DO - 10.1039/c6dt04862e ER -
@article{ author = "Warżajtis, Beata and Glišić, Biljana Đ. and Savić, Nada D. and Pavić, Aleksandar and Vojnović, Sandra and Veselinović, Aleksandar and Nikodinović-Runić, Jasmina and Rychlewska, Urszula and Đuran, Miloš I.", year = "2017", abstract = "Gold(III) complexes with different L-histidine-containing dipeptides, [Au(Gly-L-His-N-A,N-P,N3)Cl]Cl center dot 3H(2)O (1a), [Au(Gly-L-His-N-A,N-P,N-3)Cl]NO3 center dot 1.25H(2)O (1b), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (2a), [Au(L-Ala-L-His-N-A,N-P,N-3)Cl]NO3 center dot 2.5H(2)O (2b), [Au(L-Val-L-His-N-A,N-P,N-3)Cl]Cl center dot 2H(2)O (3), [Au(L-Leu-L-His-N-A,N-P,N-3)Cl]Cl (4a) and [Au(L-Leu-L-His-N-A,N-P,N-3)Cl][AuCl4]center dot H2O (4b), have been synthesized and structurally characterized by spectroscopic (1H NMR, IR and UV-vis) and single-crystal X-ray diffraction techniques. The antimicrobial efficiency of these gold(III) complexes, along with K[AuCl4] and the corresponding dipeptides, was evaluated against the broad panel of Gram-positive and Gram-negative bacteria and fungi, displaying their moderate inhibiting activity. Moreover, the cytotoxic properties of the investigated complexes were assessed against the normal human lung fibroblast cell line (MRC5) and two human cancer, cervix (HeLa) and lung (A549) cell lines. None of the complexes exerted significant cytotoxic activity; nevertheless complexes that did show selectivity in terms of cancer vs. normal cell lines (2a/b and 4a/b) have been evaluated using zebrafish (Danio rerio) embryos for toxicity and antiangiogenic potential. Although the gold(III) complexes achieved an antiangiogenic effect comparable to the known angiogenic inhibitors auranofin and sunitinib malate at 30-fold higher concentrations, they had no cardiovascular side effects, which commonly accompany auranofin and sunitinib malate treatment. Finally, binding of the gold(III) complexes to the active sites of both human and bacterial (Escherichia coli) thioredoxin reductases (TrxRs) was demonstrated by conducting a molecular docking study, suggesting that the mechanism of biological action of these complexes can be associated with their interaction with the TrxR active site.", publisher = "Royal Soc Chemistry, Cambridge", journal = "Dalton Transactions", title = "Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion", volume = "46", number = "8", pages = "2594-2608", doi = "10.1039/c6dt04862e" }
Warżajtis, B., Glišić, B. Đ., Savić, N. D., Pavić, A., Vojnović, S., Veselinović, A., Nikodinović-Runić, J., Rychlewska, U.,& Đuran, M. I.. (2017). Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion. in Dalton Transactions Royal Soc Chemistry, Cambridge., 46(8), 2594-2608. https://doi.org/10.1039/c6dt04862e
Warżajtis B, Glišić BĐ, Savić ND, Pavić A, Vojnović S, Veselinović A, Nikodinović-Runić J, Rychlewska U, Đuran MI. Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion. in Dalton Transactions. 2017;46(8):2594-2608. doi:10.1039/c6dt04862e .
Warżajtis, Beata, Glišić, Biljana Đ., Savić, Nada D., Pavić, Aleksandar, Vojnović, Sandra, Veselinović, Aleksandar, Nikodinović-Runić, Jasmina, Rychlewska, Urszula, Đuran, Miloš I., "Mononuclear gold(iii) complexes with l-histidine-containing dipeptides: tuning the structural and biological properties by variation of the N-terminal amino acid and counter anion" in Dalton Transactions, 46, no. 8 (2017):2594-2608, https://doi.org/10.1039/c6dt04862e . .