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 Rh2(4+) core encapsulated by the β fragment of the metallothionein protein protein.
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