Issue 3, 2015

Interactions of arene ruthenium metallaprisms with human proteins

Abstract

Interactions between three hexacationic arene ruthenium metallaprisms, [(p-cymene)6Ru6(tpt)2(dhnq)3]6+, [(p-cymene)6Ru6(tpt)2(dhbq)3]6+ and [(p-cymene)6Ru6(tpt)2(oxa)3]6+, and a series of human proteins including human serum albumin, transferrin, cytochrome c, myoglobin and ubiquitin have been studied using NMR spectroscopy, mass spectrometry and circular dichroism spectroscopy. All data suggest that no covalent adducts are formed between the proteins and the metallaprisms. Indeed, in most cases electrostatic interactions, leading to precipitation of protein-metallaprism aggregates, have been observed. In addition, with the smallest proteins, ubiquitin, myoglobin and cytochrome c, the presence of the hexacationic arene ruthenium metallaprisms induces structural changes of the proteins, as emphasized by circular dichroism. The results suggest that proteins are certainly a biological target for these metalla-assemblies.

Graphical abstract: Interactions of arene ruthenium metallaprisms with human proteins

Supplementary files

Article information

Article type
Paper
Submitted
15 okt 2014
Accepted
12 noy 2014
First published
12 noy 2014
This article is Open Access
Creative Commons BY-NC license

Org. Biomol. Chem., 2015,13, 946-953

Author version available

Interactions of arene ruthenium metallaprisms with human proteins

L. E. H. Paul, B. Therrien and J. Furrer, Org. Biomol. Chem., 2015, 13, 946 DOI: 10.1039/C4OB02194K

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