Search results for "Trypanosoma brucei rhodesiense"

showing 10 items of 16 documents

Development of Novel Peptide-Based Michael Acceptors Targeting Rhodesain and Falcipain-2 for the Treatment of Neglected Tropical Diseases (NTDs)

2017

This paper describes the development of a class of peptide-based inhibitors as novel antitrypanosomal and antimalarial agents. The inhibitors are based on a characteristic peptide sequence for the inhibition of the cysteine proteases rhodesain of Trypanosoma brucei rhodesiense and falcipain-2 of Plasmodium falciparum. We exploited the reactivity of novel unsaturated electrophilic functions such as vinyl-sulfones, -ketones, -esters, and -nitriles. The Michael acceptors inhibited both rhodesain and falcipain-2, at nanomolar and micromolar levels, respectively. In particular, the vinyl ketone 3b has emerged as a potent rhodesain inhibitor (k2nd = 67 × 106 M-1 min-1), endowed with a picomolar b…

0301 basic medicineCathepsin LAntimalarialPeptideHeLa Cell01 natural sciencesCysteine Proteinase InhibitorDipeptideDrug DiscoveryPeptide sequencechemistry.chemical_classificationTrypanocidal AgentbiologyNeglected DiseasesStereoisomerismDipeptidesTrypanocidal AgentsMAJOR CYSTEINE PROTEASE PLASMODIUM-FALCIPARUM TRYPANOSOMA-BRUCEI CONFORMATIONAL-ANALYSIS BIOLOGICAL EVALUATION HIGHLY POTENT VINYL-ESTER INHIBITORS PEPTIDOMIMETICS SUBSTRATEMolecular Docking SimulationCysteine EndopeptidasesBiochemistryMolecular MedicineHumanProteasesNeglected DiseaseStereochemistryPhenylalaninePlasmodium falciparumTrypanosoma brucei bruceiCysteine Proteinase InhibitorsMolecular Dynamics SimulationTrypanosoma bruceiAntimalarialsStructure-Activity Relationship03 medical and health sciencesparasitic diseasesHumansStructure–activity relationship010405 organic chemistryDrug Discovery3003 Pharmaceutical ScienceHydrogen BondingTrypanosoma brucei rhodesiensePlasmodium falciparumbiology.organism_classificationMalaria0104 chemical sciencesTrypanosomiasis African030104 developmental biologychemistryCarbamateCarbamatesCysteine EndopeptidaseHeLa CellsCysteineJournal of Medicinal Chemistry
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Repurposing a Library of Human Cathepsin L Ligands: Identification of Macrocyclic Lactams as Potent Rhodesain and Trypanosoma brucei Inhibitors.

2018

Rhodesain (RD) is a parasitic, human cathepsin L (hCatL) like cysteine protease produced by Trypanosoma brucei (T. b.) species and a potential drug target for the treatment of human African trypanosomiasis (HAT). A library of hCatL inhibitors was screened, and macrocyclic lactams were identified as potent RD inhibitors (Ki < 10 nM), preventing the cell-growth of Trypanosoma brucei rhodesiense (IC50 < 400 nM). SARs addressing the S2 and S3 pockets of RD were established. Three cocrystal structures with RD revealed a noncovalent binding mode of this ligand class due to oxidation of the catalytic Cys25 to a sulfenic acid (Cys–SOH) during crystallization. The P-glycoprotein efflux ratio was mea…

0301 basic medicineMaleTrypanosoma brucei rhodesienseSwineCathepsin LLactams MacrocyclicTrypanosoma bruceiCysteine Proteinase InhibitorsLigands01 natural sciencesCell LineCathepsin L03 medical and health sciencesStructure-Activity RelationshipIn vivoparasitic diseasesDrug DiscoveryHydrolaseAnimalsHumansIC50Binding SitesbiologyMolecular Structure010405 organic chemistryChemistryDrug RepositioningTrypanosoma brucei rhodesiensebiology.organism_classificationCysteine proteaseMolecular biologyTrypanocidal Agents0104 chemical sciencesRatsMice Inbred C57BLCysteine Endopeptidases030104 developmental biologyBlood-Brain Barrierbiology.proteinMolecular MedicineEffluxJournal of medicinal chemistry
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2 H-1,2,3-Triazole-Based Dipeptidyl Nitriles: Potent, Selective, and Trypanocidal Rhodesain Inhibitors by Structure-Based Design.

2018

Macrocyclic inhibitors of rhodesain (RD), a parasitic cysteine protease and drug target for the treatment of human African trypanosomiasis, have shown low metabolic stability at the macrocyclic ether bridge. A series of acyclic dipeptidyl nitriles was developed using structure-based design (PDB ID: 6EX8). The selectivity against the closely related cysteine protease human cathepsin L (hCatL) was substantially improved, up to 507-fold. In the S2 pocket, 3,4-dichlorophenylalanine residues provided high trypanocidal activities. In the S3 pocket, aromatic residues provided enhanced selectivity against hCatL. RD inhibition (Ki values) and in vitro cell-growth of Trypanosoma brucei rhodesiense (I…

0301 basic medicineTrypanosoma brucei rhodesienseStereochemistrySwineTrypanosoma cruziPlasmodium falciparumTriazoleProtozoan ProteinsCysteine Proteinase InhibitorsLigands01 natural sciencesCysteine Proteinase InhibitorsCell LineCathepsin L03 medical and health scienceschemistry.chemical_compoundMiceStructure-Activity RelationshipIn vivoDrug DiscoveryNitrilesStructure–activity relationshipAnimalsHumansATP Binding Cassette Transporter Subfamily B Member 1Trypanocidal agentBinding SitesbiologyMolecular Structure010405 organic chemistryChemistryTrypanosoma brucei rhodesienseDipeptidesTriazolesCysteine proteaseTrypanocidal Agents0104 chemical sciencesRatsCysteine Endopeptidases030104 developmental biologyDrug Designbiology.proteinMicrosomes LiverMolecular MedicineFemaleLeishmania donovaniJournal of medicinal chemistry
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Bistacrines as potential antitrypanosomal agents

2017

Human African Trypanosomiasis (HAT) is caused by two subspecies of the genus Trypanosoma, namely Trypanosoma brucei rhodesiense and Trypanosoma brucei gambiense. The disease is fatal if left untreated and therapy is limited due to only five non-adequate drugs currently available. In preliminary studies, dimeric tacrine derivatives were found to inhibit parasite growth with IC50-values in the nanomolar concentration range. This prompted the synthesis of a small, but smart library of monomeric and dimeric tacrine-type compounds and their evaluation of antiprotozoal activity. Rhodesain, a lysosomal cathepsin-L like cysteine protease of T. brucei rhodesiense is essential for parasite survival a…

0301 basic medicinemedicine.drug_classTrypanosoma brucei bruceiClinical BiochemistryPharmaceutical ScienceFlavoproteinBiochemistryCell LineMiceStructure-Activity Relationship03 medical and health sciencesParasitic Sensitivity TestsOxidoreductaseparasitic diseasesDrug DiscoverymedicineAnimalsAfrican trypanosomiasisMolecular BiologyCell Proliferationchemistry.chemical_classificationDose-Response Relationship DrugMolecular StructurebiologyChemistryOrganic ChemistryTrypanosoma brucei rhodesiensemedicine.diseasebiology.organism_classificationTrypanocidal AgentsCysteine proteaseTrypanosomiasis African030104 developmental biologyBiochemistryTacrineTacrineAntiprotozoalbiology.proteinMolecular MedicineProtozoamedicine.drugBioorganic &amp; Medicinal Chemistry
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Drug combination studies of curcumin and genistein against rhodesain of Trypanosoma brucei rhodesiense

2018

Curcumin and genistein are two natural products obtained from Curcuma longa L. and soybeans, endowed with many biological properties. Within the last years they were shown to possess also a promising antitrypanosomal activity. In the present paper, we investigated the activity of both curcumin and genistein against rhodesain, the main cysteine protease of Trypanosoma brucei rhodesiense; drug combination studies, according to Chou and Talalay method, allowed us to demonstrate a potent synergistic effect for the combination curcumin-genistein. As a matter of fact, with our experiments we observed that the combination index of curcumin-genistein is < 1 for the reduction from 10 to 90% of rhode…

Drugbiology010405 organic chemistryChemistrymedia_common.quotation_subjectOrganic Chemistryfood and beveragesGenisteinTrypanosoma brucei rhodesienseCombination indexPlant SciencePharmacologybiology.organism_classification01 natural sciencesBiochemistryCysteine protease0104 chemical sciencesAnalytical Chemistry010404 medicinal & biomolecular chemistrychemistry.chemical_compoundBiological propertyCurcuminCurcumin genistein rhodesain drug combination studies synergismCurcumamedia_commonNatural Product Research
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Peptidyl Vinyl Ketone Irreversible Inhibitors of Rhodesain: Modifications of the P2 Fragment.

2020

In this paper, we report the design, synthesis and biological investigation of a series of peptidyl vinyl ketones obtained by modifying the P2 fragment of previously reported highly potent inhibitors of rhodesain, the main cysteine protease of Trypanosoma brucei rhodesiense. Investigation of the structure-activity relationship led us to identify new rhodesain inhibitors endowed with an improved selectivity profile (a selectivity index of up to 22 000 towards the target enzyme), and/or an improved antitrypanosomal activity in the sub-micromolar range.

KetoneStereochemistryTrypanosoma brucei bruceiTrypanosoma bruceiCysteine Proteinase Inhibitors01 natural sciencesBiochemistrycathepsin LCathepsin LStructure-Activity RelationshipParasitic Sensitivity TestsDrug DiscoveryTrypanosoma bruceiGeneral Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationrhodesainbiologyDose-Response Relationship DrugMolecular Structure010405 organic chemistryOrganic ChemistryselectivityTrypanosoma brucei rhodesienseKetonesbiology.organism_classificationCysteine proteaseTrypanocidal Agents0104 chemical sciences010404 medicinal & biomolecular chemistryCysteine EndopeptidasesEnzymechemistrybiology.proteinMolecular MedicineMichael acceptorSelectivityPeptidesChemMedChem
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Fluorovinylsulfones and -Sulfonates as Potent Covalent Reversible Inhibitors of the Trypanosomal Cysteine Protease Rhodesain: Structure–Activity Rela…

2021

Rhodesain is a major cysteine protease of Trypanosoma brucei rhodesiense, a pathogen causing Human African Trypanosomiasis, and a validated drug target. Recently, we reported the development of α-halovinylsulfones as a new class of covalent reversible cysteine protease inhibitors. Here, α-fluorovinylsulfones/-sulfonates were optimized for rhodesain based on molecular modeling approaches. 2d, the most potent and selective inhibitor in the series, shows a single-digit nanomolar affinity and high selectivity toward mammalian cathepsins B and L. Enzymatic dilution assays and MS experiments indicate that 2d is a slow-tight binder (Ki = 3 nM). Furthermore, the nonfluorinated 2d-(H) shows favorabl…

MaleBiodistributionVinyl CompoundsMolecular modelTrypanosoma brucei bruceiCysteine Proteinase InhibitorsMiceStructure-Activity RelationshipParasitic Sensitivity TestsIn vivoDrug DiscoveryAnimalsHumansStructure–activity relationshipSulfonesEnzyme Assayschemistry.chemical_classificationMolecular StructureChemistryTrypanosoma brucei rhodesienseTrypanocidal AgentsCysteine proteaseMolecular Docking SimulationCysteine EndopeptidasesKineticsEnzymeBiochemistryCovalent bondMolecular MedicineFemaleSulfonic AcidsHeLa CellsProtein BindingJournal of Medicinal Chemistry
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Synthesis of 3-azabicyclo[3.2.2]nonanes and their antiprotozoal activities.

2015

Several bicyclic compounds, 3-azabicyclo[3.2.2]nonanes, have been prepared. The new compounds were tested for their activities against one strain of the causative organism of Malaria tropica, Plasmodium falciparum K1, which is resistant against chloroquine and pyrimethamine. In addition, their cytotoxicity and their activity against the pathogen of the East African form of sleeping sickness, Trypanosoma brucei rhodesiense, were investigated. Structure-activity relationships are discussed considering data of readily prepared compounds. For the first time, a distinct in vivo activity was observed against Plasmodium berghei in a mouse model. The active compound was further investigated.

MaleTrypanosoma brucei rhodesiensemedicine.drug_classPlasmodium bergheiClinical BiochemistryPlasmodium falciparumAntiprotozoal AgentsPharmaceutical ScienceAdministration OralBiochemistryMiceStructure-Activity RelationshipParasitic Sensitivity TestsChloroquineparasitic diseasesDrug DiscoverymedicineAnimalsPlasmodium bergheiTissue DistributionMolecular BiologyPathogenbiologyBicyclic moleculeDose-Response Relationship DrugMolecular StructureChemistryOrganic ChemistryPlasmodium falciparumTrypanosoma brucei rhodesiensebiology.organism_classificationRatsDisease Models AnimalPyrimethamineTrypanosomiasis AfricanBiochemistryInjections IntravenousAntiprotozoalMolecular MedicineAzabicyclo Compoundsmedicine.drugBioorganicmedicinal chemistry letters
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Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

2021

AbstractRhodesain is the lysosomal cathepsin L-like cysteine protease ofT. brucei rhodesiense, the causative agent of Human African Trypanosomiasis. The enzyme is essential for the proliferation and pathogenicity of the parasite as well as its ability to overcome the blood-brain barrier of the host. Lysosomal cathepsins are expressed as zymogens with an inactivating pro-domain that is cleaved under acidic conditions. A structure of the uncleaved maturation intermediate from a trypanosomal cathepsin L-like protease is currently not available. We thus established the heterologous expression ofT. brucei rhodesiensepro-rhodesain inE. coliand determined its crystal structure. The trypanosomal pr…

Models MolecularTrypanosoma brucei rhodesiense0301 basic medicinemedicine.medical_treatmentBiochemistrycysteine proteaseproenzymefluorescence correlation spectroscopy (FCS)Trypanosoma bruceiBBB blood–brain barrierCD circular dichroismchemistry.chemical_classificationEnzyme PrecursorsbiologyChemistryhsCathL human cathepsin LHydrogen-Ion ConcentrationCysteine proteaseFCS fluorescence correlation spectroscopyCysteine EndopeptidasesBiochemistryHAT Human African TrypanosomiasisNTD neglected tropical diseaseResearch Articlecrystal structureProteasesSEC size-exclusion chromatographyPET-FCS photoinduced electron transfer–fluorescence correlation spectroscopyAfrican Sleeping SicknessTrypanosoma bruceiCleavage (embryo)03 medical and health sciencesTbCathB T. brucei cathepsin BProtein DomainsZymogenmedicineMolecular BiologyzymogenrhodesainCathepsinProtease030102 biochemistry & molecular biologyActive siteTrypanosoma brucei rhodesienseCell Biologybiology.organism_classificationmolecular dynamicsEnzyme ActivationEnzyme030104 developmental biologybiology.proteinautoinhibitionHeterologous expressionJournal of Biological Chemistry
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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
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