@conference{
author = "Janjić, Goran and Bondžić, Aleksandra and Zarić, Božidarka and Čolović, Mirjana and Vasić, Vesna",
year = "2017",
abstract = "The mechanisms of anticancer action of gold(III) complexes are still largely unexplored but appear to differ profoundly from cisplatin. There are several reports that some anticancer gold(III) complexes inhibit Na/K-ATPase activity. The docking studies predicted the binding sites for tested mononuclear and oxo-bridged binuclear gold(III) complexes (Figure) in the enzyme structures, in good accordance with the results obtained by experimental measurements. All gold complexes inhibited the enzyme activity in a concentration-dependent manner achieving IC50 values in the low micromolar range. The mechanism of Na/K ATPase inhibition by AubipyC and Aubipy(OH) is similar to that of cardiotonic steroids (Na/K exchange channel), while Aupy(OAc)2 appears to block the K+ binding site. The inhibitory actions of oxo-bridged binuclear complexes are related to E2-P enzyme conformation, by binding to exchange channel and intracellular part between N and P subdomains.",
journal = "New avenues in molecular theories: From the lab to beyond the Earth : Joint Training School of the COST actions : Book of abstracts",
title = "The influence of gold(III) complexes on the Na/K-ATPase activity",
pages = "52-52",
url = "https://hdl.handle.net/21.15107/rcub_vinar_12980"
}