Search results for "Cysteine Proteinase Inhibitors"

showing 10 items of 45 documents

Development of novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation.

2015

Novel dipeptide-like rhodesain inhibitors containing the 3-bromoisoxazoline warhead in a constrained conformation were developed; some of them possess K(i) values in the micromolar range. We studied the structure-activity relationship of these derivatives and we performed docking studies, which allowed us to find out the key interactions established by the inhibitors with the target enzyme. Biological results indicate that the nature of the P2 and P3 substituents and their binding to the S2/S3 pockets is strictly interdependent.

InhibitorMolecular modelCell SurvivalClinical BiochemistryTrypanosoma brucei bruceiAntiprotozoal AgentsPharmaceutical ScienceMolecular modelingCysteine Proteinase InhibitorsBiochemistryCell Linechemistry.chemical_compoundMiceStructure-Activity RelationshipCysteine ProteasesDrug DiscoveryAnimalsMolecular Biology3-Bromo isoxazolinechemistry.chemical_classificationDipeptide-likeDipeptideBinding SitesOrganic ChemistryDipeptidesIsoxazolesCombinatorial chemistryProtein Structure TertiaryMolecular Docking SimulationCysteine EndopeptidasesEnzymeRhodesainchemistryWarheadDocking (molecular)Drug DesignMolecular MedicineRhodesain Dipeptide-like 3-Bromo isoxazoline Inhibitor Molecular modelingBioorganicmedicinal chemistry
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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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Identification of HSP90 as a new GABARAPL1 (GEC1)-interacting protein

2011

GABARAPL1 belongs to the small family of GABARAP proteins (including GABARAP, GABARAPL1 and GABARAPL2/GATE-16), one of the two subfamilies of the yeast Atg8 orthologue. GABARAPL1 is involved in the intracellular transport of receptors, via an interaction with tubulin and GABA(A) or kappa opioid receptors, and also participates in autophagy and cell proliferation. In the present study, we identify the HSP90 protein as a novel interaction partner for GABARAPL1 using GST pull-down, mass spectrometry and coimmunoprecipitation experiments. GABARAPL1 and HSP90 partially colocalize in MCF-7 breast cancer cells overexpressed Dsred-GABARAPL1 and in rat brain. Moreover, treatment of MCF-7 cells overe…

LeupeptinsLactams MacrocyclicGABARAPATG8Blotting WesternLactacystinCysteine Proteinase InhibitorsBiologyBiochemistryMass SpectrometryCell Linechemistry.chemical_compoundCell Line TumorMG132BenzoquinonesAnimalsHumansImmunoprecipitationHSP90 Heat-Shock ProteinsReceptorAdaptor Proteins Signal TransducingMicroscopy ConfocalHEK 293 cellsGeneral MedicineHsp90RatsBiochemistrychemistryProteasomebiology.proteinMicrotubule-Associated ProteinsBiochimie
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Novel combination of celecoxib and proteasome inhibitor MG132 provides synergistic antiproliferative and proapoptotic effects in human liver tumor ce…

2010

Molecular targeted therapy has shown promise as a treatment for advanced hepatocellular carcinoma (HCC). Celecoxib (Celebrex®) exhibits antitumor effects in human HCC cells, and its mechanism of action is mediated either by its ability to inhibit cyclooxygenase 2 (COX-2) or by a number of various other COX-2 independent effects. Proteasome inhibitors (PIs) can exert cell growth inhibitory and apoptotic effects in different tumor cell types, including HCC cells. The present study examined the interaction between celecoxib and the PI MG132 in two human liver tumor cell lines HepG2 and HA22T/VGH. Our data showed that each inhibitor reduced proliferation and induced apoptosis in a dose-dependen…

MG132TRB3Programmed cell deathLeupeptinsBlotting WesternApoptosisUPRPharmacologyCysteine Proteinase Inhibitorschemistry.chemical_compoundMG132medicineHumansViability assayHCCMolecular BiologyCell ProliferationSettore MED/12 - GastroenterologiaGene knockdownSulfonamidesbiologyCyclooxygenase 2 InhibitorsCell growthReverse Transcriptase Polymerase Chain ReactionDrug SynergismCell BiologyHep G2 CellsCOX-2ER stress responseFlow CytometryapoptosiproteasomechemistryApoptosisCelecoxibSettore BIO/14 - Farmacologiabiology.proteinProteasome inhibitorPyrazolesCyclooxygenaseDevelopmental Biologymedicine.drug
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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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Effects of small interfering RNAs targeting fascin on human esophageal squamous cell carcinoma cell lines

2010

Abstract Background Fascin induces membrane protrusions and cell motility. Fascin overexpression was associated with poor prognosis, and its downregulation reduces cell motility and invasiveness in esophageal squamous cell carcinoma (ESCC). Using a stable knockdown cell line, we revealed the effect of fascin on cell growth, cell adhesion and tumor formation. Methods We examined whether fascin is a potential target in ESCC using in vitro and in vivo studies utilizing a specific siRNA. We established a stable transfectant with downregulated fascin from KYSE170 cell line. Results The fascin downregulated cell lines showed a slower growth pattern by 40.3% (p In vivo, the tumor size was signific…

MaleTime FactorsHistologyEsophageal NeoplasmsMice NudeApoptosismacromolecular substancesCysteine Proteinase InhibitorsBiologyTransfectionAmino Acid Chloromethyl KetonesPathology and Forensic MedicineExtracellular matrixMiceDownregulation and upregulationCell Line TumorCell Adhesionlcsh:PathologyAnimalsHumansRNA Small InterferingCell adhesionCell ProliferationFascinMice Inbred BALB CCell growthResearchMicrofilament ProteinsGeneral MedicineTransfectionCaspase InhibitorsXenograft Model Antitumor AssaysTumor BurdenCell biologyCell cultureApoptosisCaspasesCarcinoma Squamous Cellbiology.proteinRNA InterferenceCollagenCarrier Proteinslcsh:RB1-214Diagnostic Pathology
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Optimization of Triazine Nitriles as Rhodesain Inhibitors: Structure-Activity Relationships, Bioisosteric Imidazopyridine Nitriles, and X-ray Crystal…

2013

The cysteine protease rhodesain of Trypanosoma brucei parasites causing African sleeping sickness has emerged as a target for the development of new drug candidates. Based on a triazine nitrile moiety as electrophilic headgroup, optimization studies on the substituents for the S1, S2, and S3 pockets of the enzyme were performed using structure-based design and resulted in inhibitors with inhibition constants in the single-digit nanomolar range. Comprehensive structure-activity relationships clarified the binding preferences of the individual pockets of the active site. The S1 pocket tolerates various substituents with a preference for flexible and basic side chains. Variation of the S2 subs…

Models MolecularImidazopyridineMolecular modelNitrilePyridinesStereochemistryCathepsin LTrypanosoma brucei bruceiSubstituentCysteine Proteinase InhibitorsCrystallography X-RayLigandsBiochemistryStructure-Activity Relationshipchemistry.chemical_compoundParasitic Sensitivity TestsNitrilesDrug DiscoveryHumansMoietyGeneral Pharmacology Toxicology and PharmaceuticsTriazinePharmacologyDose-Response Relationship DrugMolecular StructurebiologyTriazinesChemistryLigandOrganic ChemistryImidazolesActive siteCysteine Endopeptidasesbiology.proteinMolecular MedicineChemMedChem
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Tuning and Predicting Biological Affinity: Aryl Nitriles as Cysteine Protease Inhibitors

2012

A series of aryl nitrile-based ligands were prepared to investigate the effect of their electrophilicity on the affinity against the cysteine proteases rhodesain and human cathepsin L. Density functional theory calculations provided relative reactivities of the nitriles, enabling prediction of their biological affinity and cytotoxicity and a clear structure-activity relationship.

Models MolecularProteasesNitrileCathepsin LTrypanosoma brucei bruceiCysteine Proteinase InhibitorsBiochemistryCysteine Proteinase InhibitorsCathepsin Lchemistry.chemical_compoundCatalytic DomainNitrilesHumansOrganic chemistryPhysical and Theoretical ChemistryCathepsinbiologyArylOrganic ChemistryCombinatorial chemistryCysteine proteaseCysteine EndopeptidaseschemistryDrug Designbiology.proteinCysteineOrg. Biomol. Chem.
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Effects of E-64 (cysteine-proteinase inhibitor) and pepstatin (aspartyl-proteinase inhibitor) on metastasis formation in mice with mammary and ovaria…

1994

The effects of E-64 (Cathepsin B and L inhibitor) and Pepstatin A (Cathepsin D inhibitor) on spontaneous and experimental metastasis formation were investigated in mice with MCa mammary carcinoma, M5076 ovarian sarcoma and L1210 leukemia. Pepstatin induced a marked decrease in the number of spontaneous metastasis in MCa or M5076 tumor bearing mice. This phenomenon was also noted with E-64 but only in M5076 tumor bearing mice. On the other hand, both these agents were unable to prevent the formation of experimental metastasis in mice injected i.v. with L1210, MCa or M5076 tumor cells or with tumor cells in which Cathepsin B, L and D activities were inhibited by a 24 hour continuous exposure …

Ovarian NeoplasmsCathepsin LMammary Neoplasms ExperimentalpepstatinCysteine Proteinase Inhibitorsproteinase inhibitors.Cathepsin DCathepsinsCathepsinCathepsin BCysteine EndopeptidasesMiceLeucineEndopeptidasesPepstatinsTumor Cells CulturedAnimalsmetastasiFemaleNeoplasm MetastasisLeukemia L1210E-64In vivo (Athens, Greece)
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Caspase-dependent apoptosis during infection with Cryptosporidium parvum

1999

The protozoan parasite Cryptosporidium parvum causes persistent diarrhea and malnutrition in children and the diarrhea-wasting syndrome in AIDS. No therapy exists for eliminating the parasite in the absence of a healthy immune response. Although it had been reported that infection of intestinal cell lines with C. parvum leads to host cell death, the mechanisms of cytolysis have not been characterized. We show here that infection with C. parvum leads to typical apoptotic nuclear condensation and DNA fragmentation in host cells. Both nuclear condensation and DNA fragmentation are inhibited by a caspase inhibitor, showing that caspases are involved in this type of apoptosis. Finally, blocking …

Programmed cell deathImmunologyCryptosporidiosisApoptosisDNA FragmentationCysteine Proteinase InhibitorsMicrobiologyCaspase-Dependent ApoptosisAmino Acid Chloromethyl KetonesCell LineImmune systemparasitic diseasesAnimalsHumansComputingMilieux_MISCELLANEOUSCaspaseCryptosporidium parvumbiologybiology.organism_classificationCaspase InhibitorsVirologyCytolysisPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyInfectious DiseasesCryptosporidium parvumMicroscopy FluorescenceApoptosisCaspasesbiology.proteinDNA fragmentationHeLa CellsMicrobes and Infection
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