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

Authors :
Darabi F
Marzo T
Massai L
Scaletti F
Michelucci E
Messori L
Source :
Journal of inorganic biochemistry [J Inorg Biochem] 2015 Aug; Vol. 149, pp. 102-7. Date of Electronic Publication: 2015 Apr 01.
Publication Year :
2015

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.<br /> (Copyright © 2015 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1873-3344
Volume :
149
Database :
MEDLINE
Journal :
Journal of inorganic biochemistry
Publication Type :
Academic Journal
Accession number :
25865000
Full Text :
https://doi.org/10.1016/j.jinorgbio.2015.03.013