Ascone, Isabella, Messori, Luigi, Casini, Angela  ORCID: https://orcid.org/0000-0003-1599-9542, Gabbiani, Chiara, Balerna, Antonella, Dell'Unto, Francesca and Castellano, Agostina Congiu
2008.
Exploiting soft and hard X-ray absorption spectroscopy to characterize metallodrug/protein interactions: the binding of [trans-RuCl4(Im)(dimethylsulfoxide)][ImH] (Im = imidazole) to bovine serum albumin.
Inorganic Chemistry
47
(19)
, pp. 8629-8634.
10.1021/ic8001477
|
Abstract
The reaction of bovine serum albumin (BSA) with [trans-RuCl4(Im)(dimethylsulfoxide)][ImH] (Im = imidazole) (NAMI-A), an experimental ruthenium(III) anticancer drug, and the formation of the respective NAMI-A/BSA adduct were investigated by X-ray absorption spectroscopy (XAS) at the sulfur and chlorine K-edges and at the ruthenium K- and L3-edges. Ruthenium K and L3-edge spectra proved unambiguously that the ruthenium center remains in the oxidation state +3 after protein binding. Comparative analysis of the chlorine K-edge XAS spectra of NAMI-A and NAMI-A/BSA, revealed that the chlorine environment is greatly perturbed upon protein binding. Only modest changes were observed in the sulfur K-edge spectra that are dominated by several protein sulfur groups. Overall, valuable information on the nature of this metallodrug/protein adduct and on the mechanism of its formation was gained; XAS spectroscopy turns out to be a very suitable method for the characterization of this kind of systems.
| Item Type: | Article |
|---|---|
| Date Type: | Publication |
| Status: | Published |
| Schools: | Chemistry |
| Subjects: | Q Science > QD Chemistry |
| Publisher: | American Chemical Society |
| Last Modified: | 31 Oct 2022 08:58 |
| URI: | https://orca.cardiff.ac.uk/id/eprint/79361 |
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