Interactions between hexacationic arene ruthenium metallaprisms and the human proteins 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 electrostatic interactions, leading to precipitation of protein-metallaprism aggregates. 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.

This work was carried out in the group of PD Dr. Julien Furrer.

References:

• Lydia E. H. Paul, Bruno Therrien, Julien Furrer;
  "Interactions of arene ruthenium metallaprisms with human proteins"
  Org. Biomol. Chem., 13, 946-953, (2015); doi:10.1039/C4OB02194K.