Issue 21, 2023

Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass spectrometry

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.

Graphical abstract: Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass spectrometry

Supplementary files

Article information

Article type
Communication
Submitted
01 Feb 2023
Accepted
05 May 2023
First published
09 May 2023
This article is Open Access
Creative Commons BY-NC license

Dalton Trans., 2023,52, 6992-6996

Dirhodium tetraacetate binding to a B-DNA double helical dodecamer probed by X-ray crystallography and mass spectrometry

G. Tito, R. Troisi, G. Ferraro, A. Geri, L. Massai, L. Messori, F. Sica and A. Merlino, Dalton Trans., 2023, 52, 6992 DOI: 10.1039/D3DT00320E

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