Search results for "Trypanosoma brucei"

showing 10 items of 39 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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Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases

2017

AbstractParvulins or rotamases form a distinct group within peptidyl prolyl cis-trans isomerases. Their exact mode of action as well as the role of conserved residues in the family are still not unambiguously resolved. Using backbone S2 order parameters and NOEs as restraints, we have generated dynamic structural ensembles of three distinct parvulins, SaPrsA, TbPin1 and CsPinA. The resulting ensembles are in good agreement with the experimental data but reveal important differences between the three enzymes. The largest difference can be attributed to the extent of the opening of the substrate binding cleft, along which motional mode the three molecules occupy distinct regions. Comparison w…

0301 basic medicineFine-tuningentsyymitStaphylococcus aureusparvulinsProtein ConformationParvulinenzymesTrypanosoma brucei bruceibinding cleftIsomeraseisomerasesArticleWW domain03 medical and health sciencesHumansAmino Acid SequenceMode of actionta116Multidisciplinary030102 biochemistry & molecular biologybiologyChemistryDynamics (mechanics)ta1182Peptidylprolyl IsomeraseArchaeaNIMA-Interacting Peptidylprolyl Isomerase030104 developmental biologyOrder (biology)PIN1Biophysicsbiology.proteinProtein BindingScientific Reports
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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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Evaluation of dipeptide nitriles as inhibitors of rhodesain, a major cysteine protease of Trypanosoma brucei

2016

A series of dipeptide nitriles known as inhibitors of mammalian cathepsins were evaluated for inhibition of rhodesain, the cathepsin L-like protease of Trypanosoma brucei. Compound 35 consisting of a Leu residue fitting into the S2 pocket and a triarylic moiety consisting of thiophene, a 1,2,4-oxadiazole and a phenyl ring fitting into the S3 pocket, and compound 33 with a 3-bromo-Phe residue (S2) and a biphenyl fragment (S3) were found to inhibit rhodesain in the single-digit nanomolar range. The observed steep structure-activity relationship could be explained by covalent docking simulations. With their high selectivity indices (ca. 200) and the good antitrypanosomal activity (8μM) the com…

0301 basic medicineStereochemistrymedicine.medical_treatmentTrypanosoma brucei bruceiClinical BiochemistryAntitubercular AgentsPharmaceutical ScienceCysteine Proteinase InhibitorsTrypanosoma bruceiBiochemistryCysteine Proteinase InhibitorsStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundNitrilesDrug DiscoverymedicineStructure–activity relationshipMoietyMolecular BiologyProteaseDipeptideDose-Response Relationship DrugMolecular StructurebiologyChemistryOrganic ChemistryDipeptidesbiology.organism_classificationCysteine proteaseCysteine Endopeptidases030104 developmental biologyDocking (molecular)Molecular MedicineBioorganic &amp; Medicinal Chemistry Letters
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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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Development of novel 1,4-benzodiazepine-based Michael acceptors as antitrypanosomal agents

2016

Novel 1,4-benzodiazepines, endowed with a Michael acceptor moiety, were designed taking advantage of a computational prediction of their pharmacokinetic parameters. Among all the synthesized derivatives, we identified a new lead compound (i.e., 4a), bearing a vinyl ketone warhead and endowed with a promising antitrypanosomal activity against Trypanosoma brucei brucei (IC50 = 5.29 µM), coupled with a lack of cytotoxicity towards mammalian cells (TC50>100 µM).

0301 basic medicineTrypanosomaKetonePeptidomimeticPeptidomimeticStereochemistryTrypanosoma brucei bruceiClinical BiochemistryPharmaceutical ScienceTrypanosoma brucei01 natural sciencesBiochemistryCell LineBenzodiazepinesMiceStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundparasitic diseasesDrug DiscoveryAnimalsStructure–activity relationshipMoietyCytotoxicityMolecular BiologyMicrowave irradiationchemistry.chemical_classificationDose-Response Relationship DrugMolecular Structurebiology010405 organic chemistryMacrophagesOrganic Chemistrybiology.organism_classificationMichael acceptors Microwave irradiation Peptidomimetics Pharmacokinetic parameters TrypanosomaTrypanocidal Agents0104 chemical sciencesPharmacokinetic parameter030104 developmental biologychemistryMichael reactionMolecular MedicineMichael acceptorLead compoundBioorganic &amp; Medicinal Chemistry Letters
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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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Antiprotozoal and cysteine proteases inhibitory activity of dipeptidyl enoates

2018

A family of dipeptidyl enoates has been prepared and tested against the parasitic cysteine proteases rhodesain, cruzain and falcipain-2 related to sleeping sickness, Chagas disease and malaria, respectively. They have also been tested against human cathepsins B and L1 for selectivity. Dipeptidyl enoates resulted to be irreversible inhibitors of these enzymes. Some of the members of the family are very potent inhibitors of parasitic cysteine proteases displaying k2nd (M−1s−1) values of seven orders of magnitude. In vivo antiprotozoal testing was also performed. Inhibitors exhibited IC50 values in the micromolar range against Plasmodium falciparum, Trypanosoma brucei, Trypanosoma cruzi and ev…

0301 basic medicinesleeping sicknessClinical BiochemistryPharmaceutical Science01 natural sciencesBiochemistryCathepsin BinhibitorsDrug Discoverychemistry.chemical_classificationbiologyChemistryDipeptidesHep G2 CellsMolecular Docking SimulationCysteine EndopeptidasesBiochemistryAntiprotozoalMolecular MedicineChagas diseaseProteasesCell Survivalmedicine.drug_classPlasmodium falciparumTrypanosoma brucei bruceimalariaAntiprotozoal AgentsCysteine Proteinase InhibitorsTrypanosoma bruceicysteine proteasesInhibitory Concentration 50Structure-Activity Relationship03 medical and health sciencesparasitic diseasesmedicineHumansTrypanosoma cruziMolecular Biologychagas diseaseBinding Sites010405 organic chemistryOrganic ChemistryPlasmodium falciparumbiology.organism_classificationmedicine.diseaseProtein Structure Tertiary0104 chemical sciences030104 developmental biologyEnzymeCysteineBioorganic &amp; Medicinal Chemistry
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Promising trypanocidal heterocyclic compounds of natural origin and their synthetic analogs

2019

Abstract Diseases caused by members of the order Trypanosomatidae include human African trypanosomiasis (HAT) and Chagas disease, caused by species of Trypanosoma brucei and Trypanosoma cruzi, respectively, as well as leishmaniasis, caused by various species of Leishmania spp. These infections belong to the so-called neglected tropical diseases group, which are a diverse group of communicable diseases that prevail in tropical and subtropical conditions in 149 countries and affect more than one billion people in addition to costing developing economies billions of dollars every year. The available pharmacotherapies for combatting these diseases are limited and associated with strong side eff…

Chagas diseasebiologyTraditional medicineAntiparasiticmedicine.drug_classLeishmaniasisTrypanosoma bruceimedicine.diseasebiology.organism_classificationparasitic diseasesmedicineNeglected tropical diseasesAfrican trypanosomiasisTrypanosoma cruziTrypanosomiasis
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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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