Search results for "Cysteine Endopeptidase"

showing 10 items of 90 documents

Computer-guided drug repurposing: Identification of trypanocidal activity of clofazimine, benidipine and saquinavir

2015

In spite of remarkable advances in the knowledge on Trypanosoma cruzi biology, no medications to treat Chagas disease have been approved in the last 40 years and almost 8 million people remain infected. Since the public sector and non-profit organizations play a significant role in the research efforts on Chagas disease, it is important to implement research strategies that promote translation of basic research into the clinical practice. Recent international public-private initiatives address the potential of drug repositioning (i.e. finding second or further medical uses for known-medications) which can substantially improve the success at clinical trials and the innovation in the pharmac…

MaleDihydropyridinesProtein ConformationTrypanosoma cruziProtozoan ProteinsPharmacologyClofazimineDRUG REPOSITIONINGClofazimineMicechemistry.chemical_compoundDrug DiscoverymedicineAnimalsCLOFAZIMINESaquinavirPharmacologybusiness.industryCHAGAS DISEASEOtras Ciencias QuímicasOrganic ChemistrySAQUINAVIRDrug RepositioningCiencias QuímicasGeneral MedicineTrypanocidal AgentsBENIDIPINEMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningchemistryBenidipineFemalebusinessSaquinavirCIENCIAS NATURALES Y EXACTASmedicine.drug
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Immunoproteasome LMP2 60HH Variant Alters MBP Epitope Generation and Reduces the Risk to Develop Multiple Sclerosis in Italian Female Population

2010

BackgroundAlbeit several studies pointed out the pivotal role that CD4+T cells have in Multiple Sclerosis, the CD8+ T cells involvement in the pathology is still in its early phases of investigation. Proteasome degradation is the key step in the production of MHC class I-restricted epitopes and therefore its activity could be an important element in the activation and regulation of autoreactive CD8+ T cells in Multiple Sclerosis.Methodology/principal findingsImmunoproteasomes and PA28-alphabeta regulator are present in MS affected brain area and accumulated in plaques. They are expressed in cell types supposed to be involved in MS development such as neurons, endothelial cells, oligodendroc…

MaleT cells proteasomes multiple sclerosis parietal lobeMuscle ProteinsImmunoproteasomeEpitopeEpitopesGene FrequencyRisk FactorsCytotoxic T cellFunding: This work was financed in part by the grant Giovani Ricercatori 2007 from Italian Ministry of Health to MM DG and FMB by a grant from the European Commission Integrated Project PROTEOMAGE (FP6) to CF by the finalized projects of Fondazione Italiana Sclerosi Multipla (FISM) cod. 2003/R26 and BioPharmaNet to CF and 2002/R/40 and 2005/R/10 2008/R/11 (Genoa) to SD'A by the University of Bologna (FRO) to MPF by the Regione Piemonte (Ricerca Sanitaria Finalizzata Project and Ricerca Sanitaria Applicata-CIPE Project) to SD'A by Associazione Amici del Centro Dino Ferrari and IRCCS Ospedale Maggiore Policlinico Milano to DG and by the grants Sonderforschungsbereich (SFB-507 SFB-421) to PMK and US the grants TR43 and Neurocure to PMK. MM benefited from the A.V. Humboldt PostDoc fellowship. The funders had no role in study design data collection and analysis decision to publish or preparation of the manuscript.MultidisciplinaryMicrogliaQRBrainMiddle AgedImmunohistochemistryCysteine EndopeptidasesOligodendrogliamedicine.anatomical_structureItalyImmunoproteasome; multiple sclerosis; italian populationmultiple sclerosiImmunology/Antigen Processing and RecognitionMedicineFemaleMicrogliaNeuroscience/Neurobiology of Disease and RegenerationResearch ArticleProtein BindingAdultProteasome Endopeptidase ComplexMultiple SclerosisGenotypeScienceMolecular Sequence DataImmunology/AutoimmunityBiologySex FactorsMHC class IHLA-A2 AntigenmedicineHumansAmino Acid SequenceAlleleHLA-A AntigensMultiple sclerosisMacrophagesMyelin Basic Proteinmedicine.diseaseMyelin basic proteinImmunologybiology.proteinitalian populationCD8PLoS ONE
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In Silico Insights into the SARS CoV-2 Main Protease Suggest NADH Endogenous Defences in the Control of the Pandemic Coronavirus Infection

2020

COVID-19 is a pandemic health emergency faced by the entire world. The clinical treatment of the severe acute respiratory syndrome (SARS) CoV-2 is currently based on the experimental administration of HIV antiviral drugs, such as lopinavir, ritonavir, and remdesivir (a nucleotide analogue used for Ebola infection). This work proposes a repurposing process using a database containing approximately 8000 known drugs in synergy structure- and ligand-based studies by means of the molecular docking and descriptor-based protocol. The proposed in silico findings identified new potential SARS CoV-2 main protease (MPRO) inhibitors that fit in the catalytic binding site of SARS CoV-2 MPRO. Several sel…

Models Molecular0301 basic medicineAgingmedicine.medical_treatmentcoronaviruslcsh:QR1-502Viral Nonstructural Proteinsmedicine.disease_causelcsh:Microbiology0302 clinical medicineSettore BIO/10 - BiochimicaCoronavirus 3C ProteasesCoronavirusvirus diseasesLopinavirHypothesisMolecular Docking SimulationCysteine EndopeptidasesDrug repositioningInfectious Diseases030220 oncology & carcinogenesisCoronavirus InfectionsOxidation-Reductionmedicine.drugDNA damageIn silicoPneumonia ViralBiologyAntiviral AgentsHIV-proteaseBetacoronavirus03 medical and health sciencesSARS-CoV-2 main proteaseVirologymedicineHumansComputer SimulationProtease InhibitorsPandemicsBinding SitesProteaseSARS-CoV-2Drug RepositioningCOVID-19HIV Protease InhibitorsDRUDIT web servicemolecular dockingNADbiology.organism_classificationVirologySettore CHIM/08 - Chimica FarmaceuticaCOVID-19 Drug Treatmentcoronaviru030104 developmental biologyNADHRitonavirBetacoronavirusDNA Damage
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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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Evidence for substrate binding-induced zwitterion formation in the catalytic Cys-His dyad of the SARS-CoV main protease.

2014

The coronavirus main protease (M(pro)) represents an attractive drug target for antiviral therapy of coronavirus (CoV) infections, including severe acute respiratory syndrome (SARS). The SARS-CoV M(pro) and related CoV proteases have several distinct features, such as an uncharged Cys-His catalytic dyad embedded in a chymotrypsin-like protease fold, that clearly separate these enzymes from archetypical cysteine proteases. To further characterize the catalytic system of CoV main proteases and to obtain information about improved inhibitors, we performed comprehensive simulations of the proton-transfer reactions in the SARS-CoV M(pro) active site that lead to the Cys(-)/His(+) zwitterionic st…

Models MolecularProteasesStereochemistryvirusesmedicine.medical_treatmentEntropyStatic ElectricityMolecular Dynamics Simulationmedicine.disease_causeBiochemistrySubstrate Specificitychemistry.chemical_compoundViral ProteinsCatalytic DomainmedicineHistidineCysteineHistidineCoronavirus 3C ProteasesCoronaviruschemistry.chemical_classificationProteasebiologyChemistryvirus diseasesActive siteCysteine EndopeptidasesEnzymeBiochemistryZwitterionbiology.proteinCysteineBiochemistry
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Sortase A Inhibitors: Recent Advances and Future Perspectives

2015

Here, we describe the most promising small synthetic organic compounds that act as potent Sortase A inhibitors and cater the potential to be developed as antivirulence drugs. Sortase A is a polypeptide of 206 amino acids, which catalyzes two sequential reactions: (i) thioesterification and (ii) transpeptidation. Sortase A is involved in the process of bacterial adhesion by anchoring LPXTG-containing proteins to lipid II. Sortase A inhibitors do not affect bacterial growth, but they restrain the virulence of pathogenic bacterial strains, thereby preventing infections caused by Staphylococcus aureus or other Gram-positive bacteria. The efficacy of the most promising inhibitors needs to be com…

Models MolecularStaphylococcus aureusRhodanineProtein ConformationVirulenceAdamantanemedicine.disease_causeStaphylococcal infectionsSettore BIO/19 - Microbiologia GeneraleBenzoatesBacterial AdhesionSortase A inhibitors review future perspectiveMicrobiologySmall Molecule LibrariesBacterial ProteinsIn vivoDrug DiscoveryNitrilesmedicineAnimalsHumansEnzyme Inhibitorschemistry.chemical_classificationLipid IIbiologyThionesStaphylococcal Infectionsbiology.organism_classificationmedicine.diseaseAminoacyltransferasesSettore CHIM/08 - Chimica FarmaceuticaAmino acidAnti-Bacterial AgentsCysteine EndopeptidasesThiazolesBiochemistrychemistryStaphylococcus aureusSortase AMolecular MedicineBacteriaCarbolines
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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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Candidate Targets for Hepatitis C Virus-Specific Antiviral Therapy

1997

The hepatitis C virus (HCV) was identified as the major causative agent of posttransfusion and community-acquired non-A, non-B hepatitis throughout the world. It is an enveloped virus with a plus-strand RNA genome encoding a polyprotein of about 3,010 amino acids. This polyprotein is cleaved co- and posttranslationally into mature viral proteins by host cell signal peptidases and 2 viral enzymes designated the NS2-3 proteinase and the NS3/4A proteinase complex. It is assumed that virus replication takes place in a membrane-associated complex containing at least 2 viral enzymatic activities: the NS3 nucleoside triphosphatase (NTPase)/helicase and the NS5B RNA-dependent RNA polymerase (RdRp).…

Models MolecularvirusesHepatitis C virusHepacivirusViral Nonstructural ProteinsBiologyVirus Replicationmedicine.disease_causechemistry.chemical_compoundViral life cycleViral envelopeVirologyRNA polymeraseEndopeptidasesmedicineHumansNS5BNS3DNA Helicasesvirus diseasesRNAbiochemical phenomena metabolism and nutritionRNA-Dependent RNA PolymeraseVirologydigestive system diseasesCysteine EndopeptidasesInfectious DiseaseschemistryViral replicationIntervirology
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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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