Issue 33, 2016

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

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

Supplementary files

Article information

Article type
Communication
Submitted
15 Dec 2015
Accepted
27 Mar 2016
First published
29 Mar 2016

Chem. Commun., 2016,52, 5698-5701

Author version available

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

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