ACS Medicinal Chemistry Letters · 2016 · 28 citations · 17 references
PharmacyMedicinal ChemistryPharmacologyDrug DesignDrug DiscoveryLead OptimizationAntiviral AgentsAntiviral PharmacologyAntiviral TherapyEnzyme InhibitionLigand BindingPotency OptimizationAntiviral Drug DesignAntiviral Structure-activity RelationshipsEnzyme Activity PotencyMorpholine ChemistryProtease InhibitorsViral Protease Inhibition
A novel HIV protease inhibitor was designed using a morpholine core as the aspartate binding group. Analysis of the crystal structure of the initial lead bound to HIV protease enabled optimization of enzyme potency and antiviral activity. This afforded a series of potent orally bioavailable inhibitors of which MK-8718 was identified as a compound with a favorable overall profile.
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Andrea Cavalli, Elisabetta Poluzzi, Fabrizio De Ponti et al. · Journal of Medicinal Chemistry · 2002 · 385 citations · Full text