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Published on: July 27, 2022
Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass
Gabriella Tito1, Romualdo Troisi1, Giarita Ferraro1
1Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant'Angelo via Cintia, I-80126 Napoli, Italy. antonello.merlino@unina.it.
Abstract:
The reaction of the cytotoxic compound dirhodium tetraacetate with a B-DNA double helical dodecamer was studied by X-ray crystallography and mass spectrometry. The structure of the dirhodium/DNA adduct reveals a dimetallic center binding to an adenine via axial coordination. Complementary information has been gained through ESI MS measurements. Comparison between the present data and those previously obtained for cisplatin indicates that the two metallodrugs react with this DNA dodecamer in a significantly different fashion.

