Medicinal gold compounds form tight adducts with the copper chaperone Atox-1: biological and pharmacological implications

Chem Commun (Camb). 2012 Dec 11;48(95):11623-5. doi: 10.1039/c2cc36610j.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Coordination Complexes / chemistry
  • Copper / metabolism*
  • Copper Transport Proteins
  • Gold / chemistry*
  • Humans
  • Metallochaperones / chemistry*
  • Metallochaperones / metabolism
  • Molecular Chaperones
  • Oxidation-Reduction

Substances

  • ATOX1 protein, human
  • Coordination Complexes
  • Copper Transport Proteins
  • Metallochaperones
  • Molecular Chaperones
  • Gold
  • Copper