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.
Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass spectrometry / Tito Gabriella; Troisi Romualdo; Ferraro Giarita; Geri Andrea; Massai Lara; Messori Luigi; Sica Filomena; Merlino Antonello.. - In: DALTON TRANSACTIONS. - ISSN 1477-9234. - ELETTRONICO. - 52:(2023), pp. 6992-6996. [10.1039/d3dt00320e]
Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass spectrometry
Ferraro Giarita;Geri Andrea;Massai Lara;Messori Luigi;Merlino Antonello.
2023
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.
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