Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 60, Issue 1, Pages 511-516Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jmedchem.6b01021
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Funding
- Deutsche Forschungsgemeinschaft [KL-1356/3-1]
- German Center for Infection Research (DZIF) [8029801911]
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A thousand-fold affinity gain is achieved by introduction of a C-terminal boronic acid moiety into dipeptidic inhibitors of the Zika, West Nile, and dengue virus proteases. The resulting compounds have K-i values in the two-digit nanomolar range, are not cytotoxic, and inhibit virus replication. Structure activity relationships and a high resolution X-ray cocrystal structure with West Nile virus protease provide a basis for the design of optimized covalent-reversible inhibitors aimed at emerging flaviviral pathogens.
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