2015
DOI: 10.1039/c4ob02194k
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Interactions of arene ruthenium metallaprisms with human proteins

Abstract: Interactions between three hexacationic arene ruthenium metallaprisms, [( p-cymene) 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… Show more

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Cited by 26 publications
(17 citation statements)
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References 61 publications
(125 reference statements)
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“…[31,35,36] Similar results were obtained with three hexacationic arene ruthenium metallaprisms and severalh uman proteins.N oc ovalent adducts are formed between the proteins and the metallaprisms, and only electrostatic interactions have been observed. [42] It is likely that DiRu-1r emains intact during encapsulation, as the compound is stable under the experimental conditions used for the encapsulationp rotocol (Supporting Information Figure S4), in agreement with previouss tructural stabilityd ata collected at both acidic and basic pH values. [34] To further confirm the presence of Ru atoms within the crystals of DiRu-1-encapsulated AFt, ICP-MS measurements were performed.…”
Section: X-ray Structure Of Diru-1-encapsulated Aftsupporting
confidence: 88%
See 1 more Smart Citation
“…[31,35,36] Similar results were obtained with three hexacationic arene ruthenium metallaprisms and severalh uman proteins.N oc ovalent adducts are formed between the proteins and the metallaprisms, and only electrostatic interactions have been observed. [42] It is likely that DiRu-1r emains intact during encapsulation, as the compound is stable under the experimental conditions used for the encapsulationp rotocol (Supporting Information Figure S4), in agreement with previouss tructural stabilityd ata collected at both acidic and basic pH values. [34] To further confirm the presence of Ru atoms within the crystals of DiRu-1-encapsulated AFt, ICP-MS measurements were performed.…”
Section: X-ray Structure Of Diru-1-encapsulated Aftsupporting
confidence: 88%
“…Similar results were obtained with three hexacationic arene ruthenium metallaprisms and several human proteins. No covalent adducts are formed between the proteins and the metallaprisms, and only electrostatic interactions have been observed …”
Section: Resultsmentioning
confidence: 99%
“…Furthermore, the planarity of urea functionalized bis-pyridyl amide linker and the nature of ruthenium complex 2 further approves the proposed structure of self-assembled metalla-rectangle 3 [64,65,66]. It is worth mentioning that the variation in symmetry elements of organic linkers and ligand to metal complex ratio afford different discrete architectures [67], for instance, self-assembly of pyridine based trigonal planar linker and half-sandwich ruthenium complex in 2:3 ratio led to ruthenium based metalla-prisms [68,69].…”
Section: Resultsmentioning
confidence: 93%
“…As part of a study, looking at the development of ruthenium cage molecules based on a 2,4,6-tris(di-2-pyridylamino)-1,3,5-triazine ligand system (Figure 1), we reported on the synthesis of star-shaped trinuclear complexes [13]. These polynuclear ruthenium organometallic compounds were shown to interact with DNA in vitro , and are also effective in binding to human proteins [14]. We had hypothesized that in a mechanism similar to what is usually proposed for mononuclear compounds, the Ru-chloride bond would hydrolyze in vitro to provide a reactive intermediate with a Ru-H 2 O bond [15–17].…”
Section: Introductionmentioning
confidence: 99%