title: Medicinal gold compounds form tight adducts with the copper chaperone Atox-1: biological and pharmacological implications.
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.
authors.affiliation: Department of Chemistry and Industrial Chemistry, Pisa, Italy.
authors.forename: Chiara
authors.initials: C
authors.lastname: Gabbiani
authors.forename: Federica
authors.initials: F
authors.lastname: Scaletti
authors.forename: Lara
authors.initials: L
authors.lastname: Massai
authors.forename: Elena
authors.initials: E
authors.lastname: Michelucci
authors.forename: Maria A
authors.initials: MA
authors.lastname: Cinellu
authors.forename: Luigi
authors.initials: L
authors.lastname: Messori
mesh_terms: D056831:Coordination Complexes / Q000737:chemistry; D003300:Copper / Q000378:metabolism*; D000079922:Copper Transport Proteins; D006046:Gold / Q000737:chemistry*; D006801:Humans; D056511:Metallochaperones / Q000737:chemistry* / Q000378:metabolism; D018832:Molecular Chaperones; D010084:Oxidation-Reduction
chemical_list: C474500:ATOX1 protein, human; D056831:Coordination Complexes; D000079922:Copper Transport Proteins; D056511:Metallochaperones; D018832:Molecular Chaperones; D006046:Gold; D003300:Copper