cytochrome-c-t has been researched along with acetyl-acetonate* in 1 studies
1 other study(ies) available for cytochrome-c-t and acetyl-acetonate
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ESI-MS studies of the reactions of novel platinum(II) complexes containing O,O'-chelated acetylacetonate and sulfur ligands with selected model proteins.
A group of mixed-ligand Pt(II) complexes bearing acetylacetonate and sulphur ligands were recently developed in the University of Lecce as a new class of prospective anticancer agents that manifested promising pharma-cological properties in preliminary in vitro and in vivo tests. Though modelled on the basis of cisplatin, these Pt(II) complexes turned out to exhibit a profoundly distinct mode of action as they were found to act mainly on non-genomic targets rather than on DNA. Accordingly, we have explored here their reactions with two representative model proteins through an established ESI-MS procedure with the aim to describe their general interaction mechanism with protein targets. A pronounced reactivity with the tested proteins was indeed documented; the nature of the resulting metallodrug-protein interactions could be characterised in depth in the various cases. Preferential binding to protein targets compared to DNA is supported by independent ICP-OES measurements. The implications of these findings are discussed. Topics: Antineoplastic Agents; Binding Sites; Chelating Agents; Cytochromes c; Humans; Hydroxybutyrates; Ligands; Molecular Structure; Organoplatinum Compounds; Pentanones; Protein Binding; Solutions; Spectrometry, Mass, Electrospray Ionization; Ubiquitin | 2017 |