The reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio. Structural and functional properties of the purified platinated species, together with their spontaneous dissociation and thermally induced denaturation, have been characterized. Platinated species preserve a significant, although reduced, ribonuclease activity. The high resistance of the dimers against dissociation and the different thermal unfolding profiles suggest a quaternary structure different from those of the well-known swapped dimers of RNase A.
Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability / Picone, Delia; Donnarumma, Federica; Ferraro, G; RUSSO KRAUSS, Irene; Fagagnini, A; Gotte, G; Merlino, Antonello. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - 146:(2015), pp. 37-43. [10.1016/j.jinorgbio.2015.02.011]
Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability.
PICONE, DELIA;DONNARUMMA, FEDERICA;Ferraro G;RUSSO KRAUSS, IRENE;MERLINO, ANTONELLO
2015
Abstract
The reaction between cis-diamminedichloroplatinum(II) (CDDP), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease (RNase A), induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio. Structural and functional properties of the purified platinated species, together with their spontaneous dissociation and thermally induced denaturation, have been characterized. Platinated species preserve a significant, although reduced, ribonuclease activity. The high resistance of the dimers against dissociation and the different thermal unfolding profiles suggest a quaternary structure different from those of the well-known swapped dimers of RNase A.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.