2. Academic Validation
  3. Reactions of model proteins with aurothiomalate, a clinically established gold(I) drug: The comparison with auranofin

Reactions of model proteins with aurothiomalate, a clinically established gold(I) drug: The comparison with auranofin

  • J Inorg Biochem. 2015 Aug:149:102-7. doi: 10.1016/j.jinorgbio.2015.03.013.
Farivash Darabi 1,  Tiziano Marzo 2,  Lara Massai 2,  Federica Scaletti 2,  Elena Michelucci 3,  Luigi Messori 4
Affiliations

Affiliations

  • 1 Department of Chemistry, Isfahan University of Technology, Isfahan 84156-83111, Iran; Laboratory of Metals in Medicine, Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.
  • 2 Laboratory of Metals in Medicine, Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy.
  • 3 Mass Spectrometry Centre (CISM), University of Florence, Via U. Schiff 6, 50019 Sesto Fiorentino, Italy.
  • 4 Laboratory of Metals in Medicine, Department of Chemistry, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Florence, Italy. Electronic address: luigi.messori@unifi.it.
PMID: 25865000 DOI: 10.1016/j.jinorgbio.2015.03.013
Abstract

Aurothiomalate (AuTm) is an old, clinically established, antiarthritic gold drug that is currently being reconsidered as a candidate drug for Cancer treatment and for Other therapeutic indications within a more general drug repositioning program. As the biological effects of gold drugs seem to be mediated, mainly, by their interactions with protein targets we have analyzed here, in detail, the metalation patterns produced by aurothiomalate in a few model proteins. In particular, the reactions of aurothiomalate with the small proteins ribonuclease A, cytochrome c and lysozyme were explored through ESI MS (electrospray ionization mass spectrometry) analysis. Notably, characteristic and rather constant features emerged in the protein metalation patterns induced by AuTm that are markedly distinct from those caused by auranofin; a non-covalent interaction mode is invoked for AuTm binding to the mentioned proteins. The affinity constants of AuTm toward the three mentioned proteins were also initially assessed. The implications of the present findings are discussed.

Keywords

Auranofin; Aurothiomalate; Mass spectrometry; Proteins.

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