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SAR QSAR Environ Res. 2018 May;29(5):409-418. doi: 10.1080/1062936X.2018.1454981.

Molecular docking revealed the binding of nucleotide/side inhibitors to Zika viral polymerase solved structures.

Author information

a Biophysics Department, Faculty of Sciences , Cairo University , Giza , Egypt.
b Quantitative Life Science Department, The Abdus Salam International Center for Theoretical Physics , Strada Costiera , Trieste , Italy.
c Faculty of Pharmacy and Pharmaceutical Sciences , University of Alberta , Edmonton , AB , Canada.
d Biochemistry Department, Faculty of Medicine and Dentistry , University of Alberta , Edmonton , AB , Canada.


A new Zika virus (ZIKV) outbreak started in 2015. According to the World Health Organization, 84 countries confirmed ZIKV infection. RNA-dependent RNA polymerase (RdRp) was an appealing target for drug designers during the last two decades. Through molecular docking, we screened 16 nucleotide/side inhibitors against ZIKV RdRp. While the mode of interaction with ZIKV is different from that in the hepatitis C virus (HCV), nucleotide/side inhibitors in this study (mostly anti-HCV) showed promising binding affinities (-6.2 to -9.7 kcal/mol calculated by AutoDock Vina) to ZIKV RdRp. Setrobuvir, YAK and, to a lesser extent, IDX-184 reveal promising results compared to other inhibitors in terms of binding ZIKV RdRp. These candidates would be powerful anti-ZIKV drugs.


NS5 solved structure; RNA-dependent RNA polymerase; Zika virus; drug protein interaction; molecular docking

[Indexed for MEDLINE]

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