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

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.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Darabi F,Marzo T,Massai L,Scaletti F,Michelucci E,Messori L

doi

10.1016/j.jinorgbio.2015.03.013

subject

Has Abstract

pub_date

2015-08-01 00:00:00

pages

102-7

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(15)00089-6

journal_volume

149

pub_type

杂志文章

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