Jump to main content
Jump to site search

Issue 33, 2016
Previous Article Next Article

Destructive interactions of dirhodium(II) tetraacetate with β metallothionein rh1a

Author affiliations

Abstract

Metal-based therapeutics are vital tools in medicine. Metal-chelating proteins can dramatically decrease drug efficacy. Dirhodium(II) tetraacetate, a potential anticancer compound, binds in vitro to 8 cysteines of the human metallothionein 1a β-fragment. Electrospray ionization mass spectrometry shows that the final product is the Rh24+ core encapsulated by the β fragment of the metallothionein protein protein.

Graphical abstract: Destructive interactions of dirhodium(ii) tetraacetate with β metallothionein rh1a

Back to tab navigation

Supplementary files

Publication details

The article was received on 15 Dec 2015, accepted on 27 Mar 2016 and first published on 29 Mar 2016


Article type: Communication
DOI: 10.1039/C5CC10319C
Author version available: Download Author version (PDF)
Citation: Chem. Commun., 2016,52, 5698-5701
  •   Request permissions

    Destructive interactions of dirhodium(II) tetraacetate with β metallothionein rh1a

    D. L. Wong and M. J. Stillman, Chem. Commun., 2016, 52, 5698
    DOI: 10.1039/C5CC10319C

Search articles by author

Spotlight

Advertisements