Literature DB >> 27305454

Oxaliplatin Binding to Human Copper Chaperone Atox1 and Protein Dimerization.

Benny D Belviso1, Angela Galliani2, Alessia Lasorsa2, Valentina Mirabelli1,3, Rocco Caliandro1, Fabio Arnesano2, Giovanni Natile2.   

Abstract

Copper trafficking proteins have been implicated in the cellular response to platinum anticancer drugs. We investigated the reaction of the chaperone Atox1 with an activated form of oxaliplatin, the third platinum drug to reach worldwide approval. Unlike cisplatin, which contains monodentate ammines, oxaliplatin contains chelated 1,2-diaminocyclohexane (DACH), which is more resistant to displacement by nucleophiles. In solution, one or two {Pt(DACH)(2+)} moieties bind to the conserved CXXC metal-binding motif of Atox1; in the latter case the two sulfur atoms likely bridging the two platinum units. At longer reaction times, a dimeric species is formed whose composition, Atox12·Pt(2+)2, indicates complete loss of the diamine ligands. Such a dimerization process is accompanied by partial unfolding of the protein. Crystallization experiments aiming at the characterization of the monomeric species have afforded, instead, a dimeric species resembling that already obtained by Boal and Rosenzweig in a similar reaction performed with cisplatin. However, while in the latter case there was only one Pt-binding site (0.4 occupancy) made of four sulfur atoms of the CXXC motifs of the two Atox1 chains in a tetrahedral arrangement, we found, in addition, a secondary Pt-binding site involving Cys41 of the B chain (0.25 occupancy). Moreover, both platinum atoms have lost their diamines. Thus, there appears to be little relationship between what is observed in solution and what is formed in the solid state. Since full occupancy of the tetrahedral cavity is a common feature of all Atox1 dimeric structures obtained with other metal ions (Cu(+), Cd(2+), and Hg(2+)), we propose that in the case of platinum, where the occupancy is only 0.4, the remaining cavities are occupied by Cu(+) ions. Experimental evidence is reported in support of the latter hypothesis. Our proposal represents a meeting point between the initial proposal of Boal and Rosenzweig (0.4 Pt occupancy) and the reinterpretation of the original crystallographic data put forward by Shabalin et al. (1 Cu occupancy), and could apply to other cases.

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Year:  2016        PMID: 27305454     DOI: 10.1021/acs.inorgchem.6b00750

Source DB:  PubMed          Journal:  Inorg Chem        ISSN: 0020-1669            Impact factor:   5.165


  4 in total

1.  Characterizing metal-binding sites in proteins with X-ray crystallography.

Authors:  Katarzyna B Handing; Ewa Niedzialkowska; Ivan G Shabalin; Misty L Kuhn; Heping Zheng; Wladek Minor
Journal:  Nat Protoc       Date:  2018-04-19       Impact factor: 13.491

Review 2.  Cellular Dynamics of Transition Metal Exchange on Proteins: A Challenge but a Bonanza for Coordination Chemistry.

Authors:  Jean-Marc Moulis
Journal:  Biomolecules       Date:  2020-11-21

3.  Protein-Based Delivery Systems for Anticancer Metallodrugs: Structure and Biological Activity of the Oxaliplatin/β-Lactoglobulin Adduct.

Authors:  Daria Maria Monti; Domenico Loreto; Ilaria Iacobucci; Giarita Ferraro; Alessandro Pratesi; Luigi D'Elia; Maria Monti; Antonello Merlino
Journal:  Pharmaceuticals (Basel)       Date:  2022-03-30

4.  Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione.

Authors:  Maria I Nardella; Antonio Rosato; Benny D Belviso; Rocco Caliandro; Giovanni Natile; Fabio Arnesano
Journal:  Int J Mol Sci       Date:  2019-09-06       Impact factor: 5.923

  4 in total

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