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Activity of rat cytosolic thioredoxin reductase is strongly decreased by trans-[bis(2-amino-5-methylthiazole)tetrachlororuthenate(III)]: First report of relevant thioredoxin reductase inhibition for a ruthenium compound

  • Pasquale Mura
  • , Mercedes Camalli
  • , Alberto Bindoli
  • , Francesca Sorrentino
  • , Angela Casini
  • , Chiara Gabbiani
  • , Maddalena Corsini
  • , Piero Zanello
  • , Maria Pia Rigobello
  • , Luigi Messori
  • IMM-CNR
  • University of Padova
  • University of Florence
  • University of Siena

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

A novel "Keppler type" ruthenium(III) compound trans-[bis(2-amino 5-methylthiazole)tetrachlororuthenate(III)] 1, of potential interest as an anticancer agent, was designed, synthesized, and characterized. Its interactions with various proteins were analyzed, including the selenoenzyme thioredoxin reductase, an emerging target for anticancer metallodrugs. The selective inhibition of the cytosolic form of this selenoenzyme was documented, this being the first report of significant thioredoxin reductase inhibition by a ruthenium compound.

Original languageEnglish
Pages (from-to)5871-5874
Number of pages4
JournalJournal of Medicinal Chemistry
Volume50
Issue number24
DOIs
StatePublished - 29 Nov 2007
Externally publishedYes

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