Abstract
Based on ESI-MS measurements, we show here that some representative cytotoxic gold(III) compounds produce stable adducts upon reaction with the copper chaperone Atox-1; notably, such adducts contain gold in the oxidation state +1. These findings are of interest to understand the intracellular metabolism of medicinal gold species and to develop new potent inhibitors of the copper trafficking system.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Coordination Complexes / chemistry
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Copper / metabolism*
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Copper Transport Proteins
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Gold / chemistry*
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Humans
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Metallochaperones / chemistry*
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Metallochaperones / metabolism
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Molecular Chaperones
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Oxidation-Reduction
Substances
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ATOX1 protein, human
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Coordination Complexes
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Copper Transport Proteins
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Metallochaperones
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Molecular Chaperones
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Gold
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Copper