Search results for "INHIBITORS"

showing 10 items of 2336 documents

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 & Medicinal Chemistry Letters
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Novel Opportunities for Cathepsin S Inhibitors in Cancer Immunotherapy by Nanocarrier-Mediated Delivery

2020

Cathepsin S (CatS) is a secreted cysteine protease that cleaves certain extracellular matrix proteins, regulates antigen presentation in antigen-presenting cells (APC), and promotes M2-type macrophage and dendritic cell polarization. CatS is overexpressed in many solid cancers, and overall, it appears to promote an immune-suppressive and tumor-promoting microenvironment. While most data suggest that CatS inhibition or knockdown promotes anti-cancer immunity, cell-specific inhibition, especially in myeloid cells, appears to be important for therapeutic efficacy. This makes the design of CatS selective inhibitors and their targeting to tumor-associated M2-type macrophages (TAM) and DC an attr…

0301 basic medicineT-Lymphocytesmedicine.medical_treatmentReview02 engineering and technologyCancer immunotherapyNeoplasmsTumor-Associated MacrophagesTumor Microenvironmentcysteine proteaseMolecular Targeted TherapySulfoneslcsh:QH301-705.5Cathepsin SAntigen PresentationDrug Carrierscysteine cathepsintumor-associated macrophage (TAM)ChemistrynanoparticleAzepinesDipeptidesGeneral Medicine021001 nanoscience & nanotechnologyGene Expression Regulation NeoplasticImmunotherapy0210 nano-technologydendritic cellAntigen presentationAntineoplastic AgentsTumor-associated macrophageM2 macrophage03 medical and health sciencesLeucinemedicineHumansProtease InhibitorsAntigen-presenting celltargetingtherapypolarizationTumor microenvironmentT cellDendritic CellsDendritic cellextracellular matrix (ECM)Cathepsinstumor associated macrophage030104 developmental biologylcsh:Biology (General)antigen presenting cellCancer researchNanoparticlesimmune suppressionNanocarriers
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Topoisomerase 1 inhibition suppresses inflammatory genes and protects from death by inflammation

2015

Unwinding DNA and unleasing inflammation Fighting infections often comes with collateral damage, which sometimes can be deadly. For instance, in septic shock, the overwhelming release of inflammatory mediators drives multi-organ failure. Rialdi et al. now report a potential new therapeutic target for controlling excessive inflammation: the DNA unwinding enzyme topoisomerase I (Top1) (see the Perspective by Pope and Medzhitov). Upon infection, Top1 specifically localizes to the promoters of pathogen-induced genes and promotes their transcription by helping to recruit RNA polymerase II. Pharmacological inhibition of Top1 in a therapeutic setting increased survival in several mouse models of s…

0301 basic medicineTranscription GeneticType IInbred C57BLmedicine.disease_causeSendai virusMicePiperidinesTranscription (biology)Influenza A virusInnate2.1 Biological and endogenous factorsPositive Transcriptional Elongation Factor BAetiologyMultidisciplinaryAzepinesStaphylococcal InfectionsEbolavirusInfectious DiseasesDNA Topoisomerases Type IInfluenza A virusEbolaHost-Pathogen InteractionsPneumonia & InfluenzaRNA Polymerase IImedicine.symptomInfectionTranscriptionStaphylococcus aureusGeneral Science & TechnologyInflammationBiologyVaccine Related03 medical and health sciencesImmune systemGeneticImmunityBiodefenseGeneticsmedicineAnimalsHumansGeneFlavonoidsInflammationInnate immune systemPreventionHEK 293 cellsImmunityInterferon-betaHemorrhagic Fever EbolaTriazolesImmunity InnateMice Inbred C57BLEmerging Infectious DiseasesGood Health and Well BeingHEK293 Cells030104 developmental biologyGene Expression RegulationImmunologyCancer researchHemorrhagic FeverCamptothecinTopoisomerase I InhibitorsTopotecanDNA TopoisomerasesScience
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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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Biological Effect of a Hybrid Anticancer Agent Based on Kinase and Histone Deacetylase Inhibitors on Triple-Negative (MDA-MB231) Breast Cancer Cells

2016

We examined the effects of the histone deacetylase inhibitor (HDACi) suberoylanilide\ud hydroxamic acid (SAHA) combined with the vascular endothelial growth factor receptor-1/2 inhibitor\ud (3Z)-5-hydroxy-3-(1H-pyrrol-2-ylmethylidene)-2,3-dihydro-1H-indol-2-one on MDA-MB-231 breast\ud cancer cells (triple-negative) in the form of both a cocktail of the separate compounds and a chemically\ud synthesized hybrid (N-hydroxy-N'-[(3Z)-2-oxo-3-(1H-pyrrol-2-ylmethylidene)-2,3-dihydro-1H-indol-\ud 5-yl]octanediamide). Comparative flow cytometric and Western blot analyses were performed on\ud cocktail- and hybrid-treated cells to evaluate cell cycle distribution, autophagy/apoptosis modulation,\ud an…

0301 basic medicineVascular Endothelial Growth Factor AIndolesCytotoxicityTriple Negative Breast Neoplasmsbreast cancer; MDA-MB231 cells; histone deacetylase inhibitor; vascular endothelial growth factor receptor-2 inhibitor; cytotoxicity; cell cycle; apoptosis; autophagy; mitochondrial metabolismHydroxamic AcidsCatalysi0302 clinical medicineBreast cancerTumor Cells CulturedCytotoxic T cellSettore BIO/06 - Anatomia Comparata E CitologiaSpectroscopyVorinostatVascular endothelial growth factor receptor-2 inhibitorApoptosis; Autophagy; Breast cancer; Cell cycle; Cytotoxicity; Histone deacetylase inhibitor; MDA-MB231 cells; Mitochondrial metabolism; Vascular endothelial growth factor receptor-2 inhibitor; Catalysis; Molecular Biology; Spectroscopy; Computer Science Applications1707 Computer Vision and Pattern Recognition; Physical and Theoretical Chemistry; Organic Chemistry; Inorganic ChemistryKinaseHistone deacetylase inhibitorapoptosisComputer Science Applications1707 Computer Vision and Pattern RecognitionGeneral MedicineCell cycleFlow CytometryComputer Science ApplicationsCell biologyMDA-MB231 cell030220 oncology & carcinogenesisFemaleQD0241Programmed cell deathmedicine.drug_classCell SurvivalBlotting WesternAntineoplastic AgentsBiologyCell cycleCatalysisArticleInorganic Chemistry03 medical and health sciencesmedicineAutophagyHumansPhysical and Theoretical ChemistryProtein Kinase InhibitorsMolecular BiologyQD0415Histone deacetylase inhibitorAutophagyOrganic ChemistryApoptosiHistone Deacetylase Inhibitors030104 developmental biologyApoptosisMitochondrial metabolismMDA-MB231 cellsHistone deacetylaseInternational Journal of Molecular Sciences; Volume 17; Issue 8; Pages: 1235
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Human-based evidence for the therapeutic potential of arginase inhibitors in cardiovascular diseases

2020

Arginase is a ubiquitous enzyme that regulates polyamine- and nitric-oxide-requiring vascular functions. It is well-established that, in mammals, arginase overactivation contributes to endothelial dysfunction, a hallmark of cardiovascular diseases. The pharmacological potential of arginase inhibition for improving vascular function is largely supported by a wide range of data from animal studies. However, caution is required before extrapolating animal data to humans because interspecies differences in arginase expression and localization have been observed. For this reason, this review presents the existing arguments from human data in favor of a role of arginase in cardiovascular diseases…

0301 basic medicine[SDV]Life Sciences [q-bio]Bioinformatics03 medical and health sciencesAnimal dataVASCULAR FUNCTIONS0302 clinical medicineDrug DiscoverymedicineHumansEnzyme InhibitorsEndothelial dysfunctionComputingMilieux_MISCELLANEOUSPharmacologyArginasebusiness.industrymedicine.disease3. Good healthArginase030104 developmental biologyCardiovascular Diseases030220 oncology & carcinogenesisEndothelium VascularAnimal studiesVascular functionbusinessDrug Discovery Today
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The histone deacetylase inhibitor SAHA induces HSP60 nitration and its extracellular release by exosomal vesicles in human lung-derived carcinoma cel…

2015

// Claudia Campanella 1, 2, * , Antonella D'Anneo 3, * , Antonella Marino Gammazza 1, 2, * , Celeste Caruso Bavisotto 1, 2 , Rosario Barone 1, 2 , Sonia Emanuele 4 , Filippa Lo Cascio 1 , Emanuele Mocciaro 1 , Stefano Fais 5 , Everly Conway De Macario 6 , Alberto J.L. Macario 2, 6 , Francesco Cappello 1, 2 , Marianna Lauricella 4 1 Department of Experimental Biomedicine and Clinical Neurosciences, Section of Human Anatomy “Emerico Luna”, University of Palermo, Palermo, Italy 2 Euro-Mediterranean Institute of Science and Technology, Palermo, Italy 3 Department of Biological, Chemical and Pharmaceutical Sciences and Technologies, Laboratory of Biochemistry, University of Palermo, Palermo, Ita…

0301 basic medicineanimal structuresLung Neoplasmsmedicine.drug_classCell SurvivalNitrosationExosomes; Histone deacetylase inhibitor; HSP60; Oxidative stress; SAHAchemical and pharmacologic phenomenaAntineoplastic AgentsApoptosisexosomesBiologyHydroxamic Acidscomplex mixturesMitochondrial Proteins03 medical and health sciencesCell Line TumorSettore BIO/10 - BiochimicamedicineHumansoxidative stressSecretionViability assayCell ProliferationVorinostatHistone deacetylase inhibitorCell growthSettore BIO/16 - Anatomia UmanaHistone deacetylase inhibitorfungiSAHAChaperonin 60MicrovesiclesHistone Deacetylase InhibitorsExosome030104 developmental biologyOncologyApoptosisImmunologyCancer researchOxidative streHSP60Histone deacetylaseProtein Processing Post-TranslationalHSP60Research Paper
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Effects of Pimozide Derivatives on pSTAT5 in K562 Cells

2017

STAT5 is a transcription factor, a member of the STAT family of signaling proteins. STAT5 is involved in many types of cancer, including chronic myelogenous leukemia (CML), in which this protein is found constitutively activated as a consequence of BCR-ABL expression. The neuroleptic drug pimozide was recently reported to act as an inhibitor of STAT5 phosphorylation and is capable of inducing apoptosis in CML cells in vitro. Our research group has synthesized simple derivatives of pimozide with cytotoxic activity and that are able to decrease the levels of phosphorylated STAT5. In this work we continued the search for novel STAT5 inhibitors, synthesizing compounds in which the benzoimidazol…

0301 basic medicineantiproliferationApoptosisPharmacologyBiochemistryAntineoplastic Agent0302 clinical medicinePimozidehemic and lymphatic diseasesDrug DiscoverySTAT5 Transcription FactorCytotoxic T cellPhosphorylationGeneral Pharmacology Toxicology and PharmaceuticsBCR-ABL-expressing leukemia; STAT5 inhibitors; antiproliferation; apoptosis; pimozideSTAT5Molecular StructurebiologyPimozidefood and beverages030220 oncology & carcinogenesisMolecular MedicinePhosphorylationHumanmedicine.drugAntineoplastic AgentsNOStructure-Activity Relationship03 medical and health sciencesK562 CellmedicineHumansTranscription factorCell ProliferationPharmacologyDose-Response Relationship DrugCell growthSTAT5 inhibitorsOrganic ChemistryApoptosiSTAT5 inhibitormedicine.disease030104 developmental biologyPharmacology Toxicology and Pharmaceutics (all)biology.proteinCancer researchBCR-ABL-expressing leukemiaDrug Screening Assays AntitumorK562 CellsK562 cellsChronic myelogenous leukemiaChemMedChem
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Blocking oestradiol synthesis pathways with potent and selective coumarin derivatives

2018

A comprehensive set of 3-phenylcoumarin analogues with polar substituents was synthesised for blocking oestradiol synthesis by 17-b-hydroxysteroid dehydrogenase 1 (HSD1) in the latter part of the sulphatase pathway. Five analogues produced 62% HSD1 inhibition at 5 mM and, furthermore, three of them produced 68% inhibition at 1 mM. A docking-based structure-activity relationship analysis was done to determine the molecular basis of the inhibition and the cross-reactivity of the analogues was tested against oestrogen receptor, aromatase, cytochrome P450 1A2, and monoamine oxidases. Most of the analogues are only modestly active with 17-b-hydroxysteroid dehydrogenase 2 – a requirement for lowe…

0301 basic medicinearomatase17-Hydroxysteroid Dehydrogenasesmedicine.drug_classStereochemistry3-imidazolecoumarinaromataasiDehydrogenaseta3111LigandsStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundstructure-activity relationship (SAR)0302 clinical medicineCoumarinsIn vivo17-β-hydroxysteroid dehydrogenase 1 (HSD1)Drug DiscoverymedicineHumansMoietyEnzyme InhibitorsAromatasePharmacologyAromatase inhibitorDose-Response Relationship DrugEstradiolMolecular StructurebiologyChemistrylcsh:RM1-950CYP1A2ta1182General MedicineCoumarin3. Good healthMolecular Docking Simulationlcsh:Therapeutics. Pharmacology030104 developmental biologyDocking (molecular)030220 oncology & carcinogenesisbiology.proteinComputer-Aided Design3-Phenylcoumarinhormones hormone substitutes and hormone antagonistsResearch PaperJournal of Enzyme Inhibition and Medicinal Chemistry
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Targeting of the Leishmania Mexicana cysteine protease CPB2.8 ΔCTE by decorated fused benzo[b] thiophene scaffold.

2016

A potent and highly selective anhydride-based inhibitor of Leishmania mexicana cysteine protease CPB2.8ΔCTE (IC50 = 3.7 μM) was identified. The details of the interaction of the ligand with the enzyme active site were investigated by NMR biomimetic experiments and docking studies. Results of inhibition assays, NMR and theoretical studies indicate that the ligand acts initially as a non-covalent inhibitor and later as an irreversible covalent inhibitor by chemoselective attack of CYS 25 thiolate to an anhydride carbonyl.

0301 basic medicinebiology010405 organic chemistryChemistryStereochemistryGeneral Chemical EngineeringActive siteGeneral ChemistryHighly selectivebiology.organism_classification01 natural sciencesCysteine proteaseLeishmania mexicana0104 chemical sciences03 medical and health scienceschemistry.chemical_compound030104 developmental biologyCovalent bondDocking (molecular)biology.proteinThiopheneDRUG DISCOVERY SOFTWARE NEWS FORCE-FIELD CATHEPSIN-L INHIBITORS OPTIMIZATION TRYPANOSOMIASIS IDENTIFICATION PROTEINASES VALIDATIONIC50
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