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Platinated oligomers of bovine pancreatic ribonuclease: Structure and stability
Delia Picone1, Federica Donnarumma1, Giarita Ferraro1
1Department of Chemical Sciences, University of Naples Federico II, Via Cintia, I-80126 Naples, Italy.
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.
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