TY  - CONF
AU  - Janjić, Goran
AU  - Bondžić, Aleksandra
AU  - Zarić, Božidarka
AU  - Čolović, Mirjana
AU  - Vasić, Vesna
PY  - 2017
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/12980
AB  - 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.
C3  - New avenues in molecular theories: From the lab to beyond the Earth : Joint Training School of the COST actions : Book of abstracts
T1  - The influence of gold(III) complexes on the Na/K-ATPase activity
SP  - 52
EP  - 52
UR  - https://hdl.handle.net/21.15107/rcub_vinar_12980
ER  - 

@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"
}

Janjić, G., Bondžić, A., Zarić, B., Čolović, M.,& Vasić, V.. (2017). The influence of gold(III) complexes on the Na/K-ATPase activity. in New avenues in molecular theories: From the lab to beyond the Earth : Joint Training School of the COST actions : Book of abstracts, 52-52.
https://hdl.handle.net/21.15107/rcub_vinar_12980

Janjić G, Bondžić A, Zarić B, Čolović M, Vasić V. The influence of gold(III) complexes on the Na/K-ATPase activity. in New avenues in molecular theories: From the lab to beyond the Earth : Joint Training School of the COST actions : Book of abstracts. 2017;:52-52.
https://hdl.handle.net/21.15107/rcub_vinar_12980 .

Janjić, Goran, Bondžić, Aleksandra, Zarić, Božidarka, Čolović, Mirjana, Vasić, Vesna, "The influence of gold(III) complexes on the Na/K-ATPase activity" in New avenues in molecular theories: From the lab to beyond the Earth : Joint Training School of the COST actions : Book of abstracts (2017):52-52,
https://hdl.handle.net/21.15107/rcub_vinar_12980 .