The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
Samo za registrovane korisnike
2020
Autori
Stanić-Vučinić, DraganaNikolić, Stefan
Vlajić, Katarina
Radomirović, Mirjana Ž.
Mihailović, Jelena
Ćirković-Veličković, Tanja
Grgurić-Šipka, Sanja
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein..., implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
Ključne reči:
Ruthenium(II)-cymene complexes / Protein metalation / Anticancer metallodrugs / Mass spectrometryIzvor:
Journal of Biological Inorganic Chemistry, 2020, 25, 2, 253-265Izdavač:
- Springer
Finansiranje / projekti:
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-H2020-810752)
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-MESTD-Basic Research (BR or ON)-172024)
- Racionalni dizajn i sinteza biološki aktivnih i koordinacionih jedinjenja i funkcionalnih materijala, relevantnih u (bio)nanotehnologiji (RS-MESTD-Basic Research (BR or ON)-172035)
Napomena:
- Peer-reviewed manuscript: http://cherry.chem.bg.ac.rs/handle/123456789/3859
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3863
DOI: 10.1007/s00775-020-01758-3
ISSN: 0949-8257
WoS: 000511069000001
Scopus: 2-s2.0-85079453693
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stanić-Vučinić, Dragana AU - Nikolić, Stefan AU - Vlajić, Katarina AU - Radomirović, Mirjana Ž. AU - Mihailović, Jelena AU - Ćirković-Veličković, Tanja AU - Grgurić-Šipka, Sanja PY - 2020 UR - https://cherry.chem.bg.ac.rs/handle/123456789/3942 AB - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles. PB - Springer T2 - Journal of Biological Inorganic Chemistry T1 - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c VL - 25 IS - 2 SP - 253 EP - 265 DO - 10.1007/s00775-020-01758-3 ER -
@article{ author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja", year = "2020", abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.", publisher = "Springer", journal = "Journal of Biological Inorganic Chemistry", title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c", volume = "25", number = "2", pages = "253-265", doi = "10.1007/s00775-020-01758-3" }
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry Springer., 25(2), 253-265. https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265. doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265, https://doi.org/10.1007/s00775-020-01758-3 . .