Korge toenaosusega kauplemise strateegiad Robert Miner

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Many antiviral drugs, and compounds in clinical trials, target the NS3 protease, but few helicase inhibitors that function as antivirals have been reported.

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This study focuses on the analysis of the mechanism by which ebselen 2-phenyl-1,2-benzisoselenazolonea compound previously shown to be a HCV antiviral agent, inhibits the NS3 helicase.

However, ebselen had no effect on the activity of the NS3 protease, even at times higher ebselen concentrations.

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At concentrations below 10 μM, the ability of ebselen to inhibit HCV helicase was reversible, but prolonged incubation of HCV helicase with higher ebselen concentrations led to irreversible inhibition and the formation of covalent adducts between ebselen and all 14 cysteines present in HCV helicase.

Ebselen analogues with sulfur replacing the selenium were just as potent HCV helicase inhibitors as ebselen, but the length of the linker between the phenyl and benzisoselenazol rings was critical.

Korge toenaosusega kauplemise strateegiad Robert Miner of the phenyl ring also affected compound potency over fold, and ebselen was CFD online-kursus far more potent helicase inhibitor than other, structurally unrelated, thiol-modifying agents. Ebselen analogues were also more effective antiviral agents, and they were less toxic to hepatocytes than ebselen.

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Although the above structure-activity relationship studies suggest that ebselen targets a specific site on NS3, we were unable to confirm binding to either the NS3 ATP binding site or nucleic acid binding cleft by examining the effects of ebselen on NS3 proteins lacking key cysteines. Presently, there are no vaccines or antiviral treatments for this disease.

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Among the possible targets to fight dengue fever is the viral NS3 protease NS3PRO, which is in part responsible for viral processing and replication. It is now widely recognized that virtual screening campaigns should consider the flexibility of target protein by using multiple active conformational states.

MD simulations had the purpose to sample, as closely as possible, the ligand binding site conformational landscape prior to inhibitor binding.

The obtained conformational MD sample was clustered into four families that, together with principal component analysis of the trajectory, demonstrated protein flexibility.

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These results allowed the description of multiple binding modes for the Bz-Nle-Lys-Arg-Arg-H inhibitor, as verified by binding plots and pair interaction analysis. This study allowed us to tackle protein flexibility in our virtual screening campaign against the dengue virus NS3 protease.

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