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J Enzyme Inhib Med Chem ; 37(1): 287-298, 2022 Dec.
Article in English | MEDLINE | ID: mdl-34894959

ABSTRACT

We synthesised and screened 18 aromatic derivatives of guanylhydrazones and oximes aromatic for their capacity to bind to dengue virus capsid protein (DENVC). The intended therapeutic target was the hydrophobic cleft of DENVC, which is a region responsible for its anchoring in lipid droplets in the infected cells. The inhibition of this process completely suppresses virus infectivity. Using NMR, we describe five compounds able to bind to the α1-α2 interface in the hydrophobic cleft. Saturation transfer difference experiments showed that the aromatic protons of the ligands are important for the interaction with DENVC. Fluorescence binding isotherms indicated that the selected compounds bind at micromolar affinities, possibly leading to binding-induced conformational changes. NMR-derived docking calculations of ligands showed that they position similarly in the hydrophobic cleft. Cytotoxicity experiments and calculations of in silico drug properties suggest that these compounds may be promising candidates in the search for antivirals targeting DENVC.


Subject(s)
Antiviral Agents/pharmacology , Capsid Proteins/antagonists & inhibitors , Dengue Virus/drug effects , Hydrazones/pharmacology , Oximes/pharmacology , Antiviral Agents/chemical synthesis , Antiviral Agents/chemistry , Capsid Proteins/metabolism , Dengue Virus/metabolism , Dose-Response Relationship, Drug , Hydrazones/chemical synthesis , Hydrazones/chemistry , Hydrophobic and Hydrophilic Interactions , Microbial Sensitivity Tests , Molecular Structure , Oximes/chemical synthesis , Oximes/chemistry , Structure-Activity Relationship
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