Effect of tunable redox behavior of bis chelate substituted 1,10-phenantroline Cu(II) complexes on its reaction with superoxide anion in DMSO. Toward a simple criterion to identify a SOD-like mechanism

Manzanera-Estrada, Mayra; Cruz-Ramírez, Marisela; Flores-Álamo, Marcos; Jimenez, J.M. Gracia y; Galindo‐Murillo, Rodrigo; García‐Ramos, Juan Carlos; Ruíz-Azuara, Lena; Ortiz‐Frade, Luis

doi:10.1016/j.jinorgbio.2017.07.013

Cited by 6 publications

(2 citation statements)

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“…It has become clear that Cu complexes can act by different mechanisms other than DNA binding; ,− namely, superoxide dismutase (SOD) mimetic activity has been attributed to some complexes as well as the ability to target intracellular redox processes and modulate ROS. ,,− Topoisomerase and proteosome are also probable targets of Cu complexes. , Proteosome inhibition or interactions with proteins involved in the cell cycle have been reported, , e.g., with tubulin, or in the cytoskeleton formation, such as integrin, or those present in the extracellular medium, like fibronectin . Cu complexes show matrix metalloproteinase inhibition properties, and the generation of ROS may also disrupt enzyme pathways and induce changes in structural proteins .…”

Section: Introductionmentioning

confidence: 99%

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Copper Complexes with 1,10-Phenanthroline Derivatives: Underlying Factors Affecting Their Cytotoxicity

et al. 2020

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The interpretation of in vitro cytotoxicity data of Cu(II)-1,10-phenanthroline (phen) complexes normally does not take into account the speciation that complexes undergo in cell incubation media and its implications in cellular uptake and mechanisms of action. We synthesize and test the activity of several distinct Cu(II)-phen compounds; up to 24 h of incubation, the cytotoxic activity differs for the Cu complexes and the corresponding free ligands, but for longer incubation times (e.g., 72 h), all compounds display similar activity. Combining the use of several spectroscopic, spectrometric, and electrochemical techniques, the speciation of Cuphen compounds in cell incubation media is evaluated, indicating that the originally added complex almost totally decomposed and that Cu(II) and phen are mainly bound to bovine serum albumin. Several methods are used to disclose relationships between structure, activity, speciation in incubation media, cellular uptake, distribution of Cu in cells, and cytotoxicity. Contrary to what is reported in most studies, we conclude that interaction with cell components and cell death involves the separate action of Cu ions and phen molecules, not [Cu(phen) n ] species. This conclusion should similarly apply to many other Cu-ligand systems reported to date.

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Section: Introductionmentioning

confidence: 99%

“…to some complexes as well as the ability to target intracellular redox processes and modulate ROS. 14,32,[51][52][53][54][55] Topoisomerase and proteosome are also probable targets of Cu-complexes. 15 16 Proteosome inhibition or interactions with proteins involved in the cell cycle have been reported, 15 49 e.g.…”

Section: Introductionmentioning

confidence: 99%