The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I)

Gustavo Salinas (1, 2) , Wei Gao , Yang Wang (3) , Mariana Bonilla (1) , Long Yu , Andrey Novikov , Veridiana Virginio , Henrique Ferreira , Marisol Vieites , Vadim Gladyshev , Dinorah Gambino (4) , Shaodong Dai

1 Institut Pasteur de Montevideo
2 UDELAR - Universidad de la República [Montevideo]
3 College of Engineering [Beijing]
4 Catedra de Quimica Inorganica, Departamento Estrella Campos

New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with AuI-MPO, a novel gold inhibitor, together with inhibition assays were performed.

Keywords: Echinococcus; flatworm; glutaredoxin; gold; selenocysteine; selenoprotein; thioredoxin glutathione reductase

Domains: Structural Biology [q-bio.BM]; Organic chemistry

Gustavo Salinas, Wei Gao, Yang Wang, Mariana Bonilla, Long Yu, et al.. The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I). Antioxidants and Redox Signaling, 2017, 27 (18), pp.1491 - 1504. ⟨10.1089/ars.2016.6816⟩. ⟨pasteur-01882359⟩