Protein-metallodrugs interactions: Effects on the overall protein structure and characterization of Au, Ru and Pt binding sites

Reactions with Proteins of Three Novel Anticancer Platinum(II) Complexes Bearing N-Heterocyclic Ligands

“…In both adduct structures, the overall protein conformation is not significantly affected by Pt binding, as frequently observed [ 16 , 17 ]. In fact, root mean square deviations in the positions of the carbon alpha atoms between the structures of the adducts and those of the metal-free proteins are within the range 0.39–0.26 Å in the case of RNase A and 0.23 Å for HEWL.…”

Au3+-Induced gel network formation of proteins

“…combination studies of X-ray crystallography, isotope labeling NMR and mass spectrometry. [33][34][35][36]…”

Interactions between mitochondria-damaging platinum(iv) prodrugs and cytochrome c

“…The studies about interactions of metallodrugs with intracellular proteins attract significant attention since they have relevant pharmacological consequences. [27][28][29][30][31][32][33][34][35][36][37][38][39] Cytochrome c is a vital mitochondrial protein that plays important roles in oxi-dative phosphorylation and apoptosis. [40][41][42] Cytochrome c is reported to facilitate the reduction of satraplatin and t,c,c-bis (acetato)diaminedichloroplatinum(IV) in the presence of the electron donor nicotinamide adenine dinucleotide (NADH).…”