Search results for "Proteinase inhibitor"

showing 10 items of 85 documents

Discovery and Biological Evaluation of Potent and Selective N-Methylene Saccharin-Derived Inhibitors for Rhomboid Intramembrane Proteases

2017

Rhomboids are intramembrane serine proteases and belong to the group of structurally and biochemically most comprehensively characterized membrane proteins. They are highly conserved and ubiquitously distributed in all kingdoms of life and function in a wide range of biological processes, including epidermal growth factor signaling, mitochondrial dynamics, and apoptosis. Importantly, rhomboids have been associated with multiple diseases, including Parkinson's disease, type 2 diabetes, and malaria. However, despite a thorough understanding of many structural and functional aspects of rhomboids, potent and selective inhibitors of these intramembrane proteases are still not available. In this …

0301 basic medicineProteasesSerine Proteinase InhibitorsChemistryRhomboid proteaseRhomboidHEK 293 cellsRational designMembrane ProteinsBiochemistryIn vitroArticleSerine03 medical and health sciences030104 developmental biologyHEK293 CellsSaccharinBiochemistryMembrane proteinDrug DesignComputer-Aided DesignHumansSerine Proteases
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Discovery and validation of 2-styryl substituted benzoxazin-4-ones as a novel scaffold for rhomboid protease inhibitors

2017

Abstract Rhomboids are intramembrane serine proteases with diverse physiological functions in organisms ranging from archaea to humans. Crystal structure analysis has provided a detailed understanding of the catalytic mechanism, and rhomboids have been implicated in various disease contexts. Unfortunately, the design of specific rhomboid inhibitors has lagged behind, and previously described small molecule inhibitors displayed insufficient potency and/or selectivity. Using a computer-aided approach, we focused on the discovery of novel scaffolds with reduced liabilities and the possibility for broad structural variations. Docking studies with the E. coli rhomboid GlpG indicated that 2-styry…

0301 basic medicineProteasesSerine Proteinase InhibitorsStereochemistrymedicine.medical_treatmentClinical BiochemistryPharmaceutical ScienceBiochemistryStyrenesSerine03 medical and health sciencesCatalytic DomainEndopeptidasesDrug DiscoveryEscherichia coliSerinemedicineAnimalsChymotrypsinDrosophila ProteinsHumansMolecular BiologyEnzyme AssaysSerine proteaseProtease030102 biochemistry & molecular biologybiologyBenzoxazinonesChemistryEscherichia coli ProteinsRhomboid proteaseRhomboidOrganic ChemistryMembrane ProteinsTransforming Growth Factor alphaBenzoxazinesDNA-Binding ProteinsMolecular Docking Simulation030104 developmental biologyDocking (molecular)Mutationbiology.proteinMolecular MedicineCattleDrosophilaBioorganic & Medicinal Chemistry Letters
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New aziridine-based inhibitors of cathepsin L-like cysteine proteases with selectivity for the Leishmania cysteine protease LmCPB2.8

2018

Abstract In the present work a series of aziridine-2,3-dicarboxylate inhibitors of papain-like cysteine proteases was designed, synthesized and tested. The compounds displayed selectivity for the parasitic protozoon Leishmania mexicana cathepsin L-like cysteine protease LmCPB2.8. The computational methods of homology modelling and molecular docking predicted some significant differences in the S2 pocket of LmCPB2.8 and cruzain, a related enzyme from Trypanosoma cruzi. Due to the presence of Tyr209 in LmCPB2.8 rather than Glu208 in cruzain sterically demanding, lipophilic ester groups (inhibitor 7d, 9d, 12d and 14d) are predicted to occupy the S2 pocket of the Leishmania protease, but do not…

0301 basic medicineProteasesStereochemistryCathepsin Lmedicine.medical_treatmentAziridinesLeishmania mexicana030106 microbiologyLeishmaniasis CutaneousCysteine Proteinase Inhibitors01 natural sciencesLeishmania mexicanaCathepsin L03 medical and health sciencesparasitic diseasesDrug DiscoverymedicineHumansLeishmaniasisLeishmaniaPharmacologyProteaseAntiparasitic Agentsbiology010405 organic chemistryChemistryOrganic ChemistryActive siteGeneral Medicinebiology.organism_classificationCysteine protease0104 chemical sciencesMolecular Docking SimulationDocking (molecular)biology.proteinCysteineEuropean Journal of Medicinal Chemistry
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Warhead Reactivity Limits the Speed of Inhibition of the Cysteine Protease Rhodesain.

2021

Viral and parasitic pathogens rely critically on cysteine proteases for host invasion, replication, and infectivity. Their inhibition by synthetic inhibitors, such as vinyl sulfone compounds, has emerged as a promising treatment strategy. However, the individual reaction steps of protease inhibition are not fully understood. Using the trypanosomal cysteine protease rhodesain as a medically relevant target, we design photoinduced electron transfer (PET) fluorescence probes to detect kinetics of binding of reversible and irreversible vinyl sulfones directly in solution. Intriguingly, the irreversible inhibitor, apart from its unlimited residence time in the enzyme, reacts 5 times faster than …

0301 basic medicineProteasesmedicine.medical_treatmentKineticsCysteine Proteinase InhibitorsLigands01 natural sciencesBiochemistryFluorescence03 medical and health sciencesReaction rate constantmedicineReactivity (chemistry)chemistry.chemical_classificationProtease010405 organic chemistryGeneral MedicineCysteine protease0104 chemical sciencesCysteine EndopeptidasesKinetics030104 developmental biologyEnzymechemistryBiophysicsMolecular MedicineCysteineACS chemical biology
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Anti-PCSK9 treatment: is ultra-low low-density lipoprotein cholesterol always good?

2018

Anti-PCSK9 (proprotein convertase subtilisin kexin 9) monoclonal antibodies (Mab) are novel, potent lipid-lowering drugs. They demonstrated to improve the lipid profile in high cardiovascular risk patients. Anti-PCSK9 Mab inhibit the targeted low-density lipoprotein (LDL)-receptor degradation induced by PCSK9 protein and are able to reduce LDL cholesterol (LDL-C) levels on top of conventional lipid-lowering therapy. Though these drugs proved to be very safe in the short-term, little is known about the possible long-term effects, due to the short period of their marketing. The genetic low cholesterol syndromes (LCS) represent the natural models of the lipid-lowering anti-PCSK9 therapy, and a…

0301 basic medicineSerine Proteinase InhibitorsTime FactorsPhysiologymedicine.drug_class030204 cardiovascular system & hematologyPharmacologyMonoclonal antibodyRisk Assessment03 medical and health sciencesPCSK9 Genechemistry.chemical_compound0302 clinical medicineRisk FactorsPhysiology (medical)Diabetes mellitusmedicineAnimalsHumansDyslipidemiasmedicine.diagnostic_testbusiness.industryCholesterolPCSK9Anticholesteremic AgentsPCSK9 InhibitorsAntibodies MonoclonalCholesterol LDLmedicine.diseaseFatty LiverHypocholesterolemia030104 developmental biologyTreatment OutcomechemistryDiabetes Mellitus Type 2lipids (amino acids peptides and proteins)Proprotein Convertase 9Cardiology and Cardiovascular MedicineLipid profilebusinessCognition DisordersBiomarkersLipoproteinCardiovascular research
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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 & 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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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 & Medicinal Chemistry
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Expression of cysteine proteinases cathepsins B and K and of cysteine proteinase inhibitor cystatin C in giant cell tumor of tendon sheath.

2001

The expression of cysteine proteinases cathepsins B and K and of the endogenous inhibitor of cysteine proteinases, cystatin C, was investigated in tissue specimens of patients with giant cell tumor of tendon sheath (GCTTS). Expression of both enzymes was examined by immunohistochemistry in tissue specimens of 14 patients with GCTTS. Applying double-labeling techniques, the coexpression of cathepsin B and its major endogenous inhibitor cystatin C was additionally studied. Cells expressing the respective proteins were further characterized with the macrophage markers HAM56 and anti-CD68 (clone PG-M1). Cathepsin B could be detected in numerous HAM56-positive mononuclear cells (MC), but only in…

AdultMaleCathepsin KAntigens Differentiation MyelomonocyticCathepsin ECell CountCathepsin FBiologyCysteine Proteinase InhibitorsGiant CellsCathepsin BPathology and Forensic MedicineCathepsin CCathepsin BImmunoenzyme TechniquesTendonsCathepsin OCathepsin HAntigens CDCathepsin L1HumansCystatin CCathepsin SAgedMuscle NeoplasmsGiant Cell TumorsAntibodies MonoclonalMiddle AgedMolecular biologyCathepsinsCystatinsBiochemistryLeukocytes MononuclearFemaleModern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc
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Low SPINK5 expression in chronic rhinosinusitis

2012

Objectives/Hypothesis: Chronic rhinosinusitis (CRS) is a multifactorial disease that probably arises as a result of genetic diversity and environmental factors. SPINK5 is a serine protease inhibitor, which is supposed to be an important regulator of epithelial barrier maintenance. The role of SPINK5 polymorphisms and expression in CRS, especially in individuals with aspirin intolerance, is unclear. Study Design: SPINK5 single-nucleotide polymorphisms (SNPs) and SPINK5 expression levels were correlated with CRS without (CRSsNP) and with nasal polyps (CRSwNP), aspirin intolerance, asthma, and allergies. Methods: One hundred four nasal tissue samples, 15 from patients with CRSsNP, 59 from pati…

AdultMalePathologymedicine.medical_specialtyAllergyAdolescentGenotypeProteinase Inhibitory Proteins SecretorySingle-nucleotide polymorphismPolymerase Chain ReactionPolymorphism Single NucleotideSensitivity and SpecificitySampling Studieslaw.inventionDrug HypersensitivityTissue Culture TechniquesYoung AdultNasal PolypsReference ValueslawGenotypemedicineHumansSNPNasal polypsRNA MessengerSinusitisPolymerase chain reactionAgedRhinitisAsthmaAged 80 and overAspirinbusiness.industryMiddle Agedmedicine.diseaseAsthmaPathophysiologyNasal MucosaGene Expression RegulationOtorhinolaryngologyChronic DiseaseImmunologySerine Peptidase Inhibitor Kazal-Type 5FemalebusinessThe Laryngoscope
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