Search results for "ADME-Tox"

showing 2 items of 2 documents

The discovery of novel antitrypanosomal 4-phenyl-6-(pyridin-3-yl)pyrimidines

2021

Human African trypanosomiasis, or sleeping sickness, is a neglected tropical disease caused by Trypanosoma brucei rhodesiense and Trypanosoma brucei gambiense which seriously affects human health in Africa. Current therapies present limitations in their application, parasite resistance, or require further clinical investigation for wider use. Our work herein describes the design and syntheses of novel antitrypanosomal 4-phenyl-6-(pyridin-3-yl)pyrimidines, with compound 13, the 4-(2-methoxyphenyl)-6-(pyridine-3-yl)pyrimidin-2-amine demonstrating an IC50 value of 0.38 μM and a promising off-target ADME-Tox profile in vitro. In silico molecular target investigations showed rhodesain to be a pu…

Models MolecularTrypanosoma brucei rhodesiensepyrimidinessleeping sicknessIn silicoHuman african trypanosomiasis01 natural sciencesDockingCell Line03 medical and health sciencesantitrypanosomalDrug DiscoverymedicineAnimalsHumansAfrican trypanosomiasisIC50030304 developmental biologyrhodesainPharmacology0303 health sciences010405 organic chemistryChemistryDrug discoveryOrganic ChemistryAntitrypanosomalSleeping sicknessTrypanosoma brucei rhodesienseGeneral MedicineHuman African Trypanosomiasismedicine.diseaseTrypanocidal AgentsIn vitroRats0104 chemical sciencesPyrimidinesRhodesainTrypanosomiasis AfricanBiochemistryDrug developmentDocking (molecular)dockingADME-ToxResearch Paper
researchProduct

Ensemble-based ADME-Tox profiling and virtual screening for the discovery of new inhibitors of the Leishmania mexicana cysteine protease CPB2.8ΔCTE

2018

Abstract: In an effort to identify novel molecular warheads able to inhibit Leishmania mexicana cysteine protease CPB2.8CTE, fused benzo[b]thiophenes and ,'-triketones emerged as covalent inhibitors binding the active site cysteine residue. Enzymatic screening showed a moderate-to-excellent activity (12%-90% inhibition of the target enzyme at 20m). The most promising compounds were selected for further profiling including in vitro cell-based assays and docking studies. Computational data suggest that benzo[b]thiophenes act immediately as non-covalent inhibitors and then as irreversible covalent inhibitors, whereas a reversible covalent mechanism emerged for the 1,3,3'-triketones with a Y-to…

Cell SurvivalLeishmania mexicanaProtozoan ProteinsADME-Tox; Benzo[b]thiophenes; Cysteine protease; Leishmaniasis; TriketonesThiophenesCysteine Proteinase Inhibitors010402 general chemistry01 natural sciencesBiochemistryLeishmania mexicanaCysteine Proteinase InhibitorsCell LineInhibitory Concentration 50Structure-Activity RelationshipCysteine ProteasesCatalytic DomainDrug DiscoveryHumansStructure–activity relationshipcysteine proteaseBinding siteADME-Tox; benzo[b]thiophenes; cysteine protease; leishmaniasis; triketones; Biochemistry; Molecular MedicineBiologyleishmaniasisPharmacologychemistry.chemical_classificationVirtual screeningBinding Sitesbiology010405 organic chemistryPharmacology. TherapyOrganic Chemistrytriketonesbiology.organism_classificationCysteine protease0104 chemical sciencesMolecular Docking SimulationChemistryEnzymeBiochemistrychemistryDocking (molecular)ADME-ToxMolecular Medicinebenzo[b]thiophenes
researchProduct