Copper binding promotes the interaction of cisplatin with human copper chaperone Atox1

Zhaoyong Xi; Wei Guo; Changlin Tian; Fuyi Wang; Yangzhong Liu

doi:10.1039/c3cc45905e

Copper binding promotes the interaction of cisplatin with human copper chaperone Atox1

Chem Commun (Camb). 2013 Dec 11;49(95):11197-9. doi: 10.1039/c3cc45905e.

Authors

Zhaoyong Xi¹, Wei Guo, Changlin Tian, Fuyi Wang, Yangzhong Liu

Affiliation

¹ CAS Key Laboratory of Soft Matter Chemistry and Department of Chemistry, University of Science and Technology of China, Hefei, Anhui, China. liuyz@ustc.edu.cn.

PMID: 24150599
DOI: 10.1039/c3cc45905e

Abstract

Cu(I) binding promotes the platination of Atox1, although cisplatin binds to the copper coordination sites. In addition, Cu(I) binding enhances the competition of Atox1 with DTT in the reaction of cisplatin. These results indicate that cuprous ions could regulate the cellular trafficking of cisplatin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cisplatin / chemistry*
Coordination Complexes / chemical synthesis
Coordination Complexes / chemistry
Copper / chemistry*
Copper Transport Proteins
Humans
Metallochaperones / chemistry*
Molecular Chaperones
Protein Binding

Substances

ATOX1 protein, human
Coordination Complexes
Copper Transport Proteins
Metallochaperones
Molecular Chaperones
cuprous ion
Copper
Cisplatin