Search results for "Leucyl Aminopeptidase"

showing 10 items of 15 documents

Phosphinotripeptidic Inhibitors of Leucylaminopeptidases

2021

Phosphinate pseudopeptide are analogs of peptides containing phosphinate moiety in a place of the amide bond. Due to this, the organophosphorus fragment resembles the tetrahedral transition state of the amide bond hydrolysis. Additionally, it is also capable of coordinating metal ions, for example, zinc or magnesium ions. These two properties of phosphinate pseudopeptides make them an ideal candidate for metal-related protease inhibitors. This research investigates the influence of additional residue in the P2 position on the inhibitory properties of phosphinopeptides. The synthetic strategy is proposed, based on retrosynthetic analysis. The N-C-P bond formation in the desired compounds is …

0106 biological sciences0301 basic medicineModels MolecularMolecular modelQH301-705.5StereochemistryPhosphinesProtein ConformationSwineLAP inhibitorsligand-enzyme interactionPhosphinate01 natural sciencesAminopeptidaseCatalysisArticleInorganic Chemistry03 medical and health sciencesResidue (chemistry)phosphinate pseudopeptideLeucyl AminopeptidaseMoietyPeptide bondAnimalsBiology (General)Physical and Theoretical ChemistryEnzyme InhibitorsQD1-999Molecular BiologyMagnesium ionmolecular modeling; LAP inhibitors; barley aminopeptidase inhibitor; phosphinate pseudopeptide; ligand-enzyme interaction; organophosphorus compoundSpectroscopyChemistrymolecular modelingOrganic ChemistryGeneral Medicineorganophosphorus compoundPeptide FragmentsComputer Science ApplicationsChemistry030104 developmental biologybarley aminopeptidase inhibitorHordeum vulgare010606 plant biology & botanyInternational Journal of Molecular Sciences; Volume 22; Issue 10; Pages: 5090
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Identification and properties of the cell membrane bound leucine aminopeptidase interacting with the potential immunostimulant and chemotherapeutic a…

1983

Bestatin was found to be a competitive inhibitor (with respect to the Leu-NA substrate) not only of the isolated microsomal and cytosolic leucine aminopeptidases (Leu-APm and Leu-APc) but also of the aminopeptidases (APs) present in membrane preparations (from mouse liver) and on the cell surface of L5178Y cells. Kinetic parameters indicate that cellular AP is identical to Leu-APm. To rule out the possibility that AP-B is involved in the inhibition reactions, comparable studies with amastatin were performed. Electrophoretical studies revealed the solubilized cell membrane bound AP to co-migrate with Leu-APm in polyacrylamide gels. The activity of the separated membrane AP was inhibited by b…

MaleSurface PropertiesCellBiochemistryAminopeptidaseBinding CompetitiveCell membranechemistry.chemical_compoundLeucyl AminopeptidaseMiceAmastatinCytosolLeucinemedicineAnimalsCells CulturedPharmacologyBinding SitesChemistryCell CycleCell MembraneCell cycleCytosolmedicine.anatomical_structureBiochemistryMicrosomeMice Inbred CBALeucineProtein BindingBiochemical pharmacology
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Structure-Guided, Single-Point Modifications in the Phosphinic Dipeptide Structure Yield Highly Potent and Selective Inhibitors of Neutral Aminopepti…

2014

Seven crystal structures of alanyl aminopeptidase from Neisseria meningitides (the etiological agent of meningitis, NmAPN) complexed with organophosphorus compounds were resolved to determine the optimal inhibitor–enzyme interactions. The enantiomeric phosphonic acid analogs of Leu and hPhe, which correspond to the P1 amino acid residues of well-processed substrates, were used to assess the impact of the absolute configuration and the stereospecific hydrogen bond network formed between the aminophosphonate polar head and the active site residues on the binding affinity. For the hPhe analog, an imperfect stereochemical complementarity could be overcome by incorporating an appropriate P1 side…

MeningitidesStereochemistryHeteroatomAminopeptidases01 natural sciencesArticleLeucyl AminopeptidaseStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundDrug DiscoveryHumansProtease Inhibitors030304 developmental biology0303 health sciencesBinding SitesDipeptidebiology010405 organic chemistryHydrogen bondAbsolute configurationActive siteLigand (biochemistry)0104 chemical scienceschemistryAminophosphonateDrug Designbiology.proteinMolecular MedicineJournal of Medicinal Chemistry
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Leucine aminopeptidase is an immunodominant antigen of Fasciola hepatica excretory and secretory products in human infections.

2007

ABSTRACT The liver fluke Fasciola hepatica parasitizes humans and ruminant livestock worldwide, and it is now being considered a reemerging zoonotic disease, especially in areas in which it is endemic, such as South America. This study investigates the immune response to excretory and secretory products produced by F. hepatica in a group of patients from the Peruvian Altiplano, where the disease is highly endemic. Using a proteomic approach and immunoblotting techniques, we have identified the enzymes leucine aminopeptidase (LAP) and phosphoenolpyruvate carboxykinase as immunodominant antigens recognized by sera from fasciolosis patients. An indirect enzyme-linked immunosorbent assay using …

Microbiology (medical)FascioliasisAdolescentClinical BiochemistryImmunologyBlotting WesternMolecular Sequence DataSheep DiseasesEnzyme-Linked Immunosorbent AssayAminopeptidasePolymerase Chain ReactionLeucyl AminopeptidaseImmune systemAntigenHepaticaparasitic diseasesmedicineImmunology and AllergyFasciola hepaticaAnimalsHumansElectrophoresis Gel Two-DimensionalFasciolosisChildDNA PrimersSheepbiologyBase SequenceImmunodominant EpitopesClinical and Diagnostic Laboratory ImmunologyLiver flukeFasciola hepaticabiology.organism_classificationmedicine.diseaseVirologyExcretory systemAntigens HelminthChild PreschoolClinical and vaccine immunology : CVI
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Antigen processing influences HIV-specific cytotoxic T lymphocyte immunodominance

2016

Udgivelsesdato: 2009-May-03 Although cytotoxic T lymphocytes (CTLs) in people infected with human immunodeficiency virus type 1 can potentially target multiple virus epitopes, the same few are recognized repeatedly. We show here that CTL immunodominance in regions of the human immunodeficiency virus type 1 group-associated antigen proteins p17 and p24 correlated with epitope abundance, which was strongly influenced by proteasomal digestion profiles, affinity for the transporter protein TAP, and trimming mediated by the endoplasmatic reticulum aminopeptidase ERAAP, and was moderately influenced by HLA affinity. Structural and functional analyses demonstrated that proteasomal cleavage 'prefer…

Models MolecularProteasome Endopeptidase ComplexHIV AntigensMolecular Sequence DataImmunologyAntigen presentationHIV Core Protein p24HIV InfectionsImmunodominanceMajor histocompatibility complexgag Gene Products Human Immunodeficiency VirusEpitopeEvolution MolecularMajor Histocompatibility ComplexLeucyl Aminopeptidase03 medical and health sciences0302 clinical medicineAntigenHumansImmunology and AllergyCytotoxic T cellAmino Acid Sequence030304 developmental biologyAntigen Presentation0303 health sciencesHLA-A AntigensbiologyImmunodominant EpitopesAntigen processingVirology3. Good healthCTL*MutationHIV-1biology.proteinATP-Binding Cassette TransportersProtein BindingT-Lymphocytes Cytotoxic030215 immunologyRETROVIROLOGY
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A synthetic method for diversification of the P1′ substituent in phosphinic dipeptides as a tool for exploration of the specificity of the S1′ bindin…

2007

Abstract A novel, general, and versatile method of diversification of the P1′ position in phosphinic pseudodipeptides, presumable inhibitors of proteolytic enzymes, was elaborated. The procedure was based on parallel derivatization of the amino group in the suitably protected phosphinate building blocks with appropriate alkyl and aryl halides. This synthetic strategy represents an original approach to phosphinic dipeptide chemistry. Its usefulness was confirmed by obtaining a series of P1′ modified phosphinic dipeptides, inhibitors of cytosolic leucine aminopeptidase, through computer-aided design basing on the structure of homophenylalanyl-phenylalanine analogue (hPheP[CH 2 ]Phe) bound in …

Models MolecularStereochemistryClinical BiochemistryLAP inhibitorsSubstituentPharmaceutical SciencePhosphinateLigandsBiochemistryAminopeptidaseLeucyl AminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundDrug DiscoveryP1′ diversificationcross-couplingMolecular BiologyalkylationBinding SitesDipeptideMolecular StructurebiologyOrganic ChemistryProteolytic enzymesActive siteHydrogen BondingStereoisomerismDipeptidesPhosphinic Acidsphosphinic pseudodipeptideschemistrybiology.proteinMolecular MedicineLeucineLead compoundBioorganic & Medicinal Chemistry
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Leucine Aminopeptidase Activity in Mast Cells

1959

DURING investigations of the behaviour of leucine aminopeptidase activity of blood-serum in patients with dermatoses and tumours1–3, in a case of diffuse skin mastocytosis of a new-born, we detected heightened activity of leucine aminopeptidase. After mechanical friction of the affected skin, greater activity of leucine aminopeptidase occurred. From this we supposed a release of leucine aminopeptidase from the mast cell infiltrates of the skin. As is well known, in urticaria pigmentosa mechanical irritation of the skin lesions give rise to a degranulation of mast cells4,5 with liberation of histamine and serotonin. Indeed, there is no doubt that mast cells contain the enzyme leucine aminope…

MultidisciplinaryBiochemical PhenomenaHydrolasesChemistryDegranulationConnective tissueMast cellmedicine.diseaseMolecular biologyAminopeptidaseLeucyl Aminopeptidasechemistry.chemical_compoundmedicine.anatomical_structureBiochemistryLeucineEndopeptidasesmedicineHumansUrticaria pigmentosaLiberationMast CellsLeucineHistaminePeptide HydrolasesNature
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Differentiation of Penicillium griseofulvum Dierckx isolates by enzyme assays and by patulin and griseofulvin analyses

1990

The production of patulin and griseofulvin by 49 different isolates of Penicillium griseofulvum Dierckx was analyzed by high-performance liquid chromatography. Eleven isolates were obtained from pistachio nuts, 37 were obtained from wheat seeds, and 1 was obtained from the American Type Culture Collection. Activities of 19 enzymes were also assayed by the API ZYM system. From these results it may be deduced that there are two different groups among the strains tested which cannot be distinguished by morphological and cultural characteristics. One group of isolates did not produce detectable amounts of patulin and griseofulvin when grown in sucrose-yeast extract and Wickerham media, while en…

Penicillium griseofulvumHydrolasesApplied Microbiology and BiotechnologyGriseofulvinPatulinLeucyl Aminopeptidasechemistry.chemical_compoundMycotoxinChromatography High Pressure LiquidEcologybiologybeta-GlucosidasePenicilliumPhosphoamidaseFungi imperfectibiology.organism_classificationGriseofulvinEnzyme assayCulture MediaPatulinchemistryBiochemistryPenicilliumbiology.proteinResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Stereoselective synthesis of 1-aminoalkanephosphonic acids with two chiral centers and their activity towards leucine aminopeptidase

2003

The stereoselective synthesis of 1-amino-2-alkylalkanephosphonic acids, namely, compounds bearing two chiral centers, was achieved by the condensation of hypophosphorous acid salts of (R)(+) or (S)(-)-N-alpha-methylbenzylamine with the appropriate aldehydes in isopropanol. Simultaneous deprotection and oxidation by the action of bromine water provided equimolar mixtures of the RS:RR and SR:SS diastereomers of desired acids. They appeared to act as moderate inhibitors of kidney leucine aminopeptidase with potency dependent on the absolute configuration of both centers of chirality.

PharmacologyHypophosphorous acidChemistryStereochemistryOrganic ChemistryOrganophosphonatesDiastereomerAbsolute configurationMetalloendopeptidasesStereoisomerismStereoisomerismAminopeptidaseCatalysisAnalytical Chemistry2-PropanolLeucyl AminopeptidaseZincchemistry.chemical_compoundModels ChemicalDrug DiscoveryStereoselectivityLeucineChirality (chemistry)SpectroscopyChirality
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A phosphonamidate containing aromatic N-terminal amino group as inhibitor of leucine aminopeptidase-design, synthesis and stability.

2006

Fully deprotected phosphonamidate dipeptides, predicted as effective inhibitors of cytosolic leucine aminopeptidase, showed unexpected instability in water solution at pH below 12. Their hydrolysis rate was strictly correlated with basicity of the N-terminal amino group. To improve this feature a phosphonamidate analogue containing less basic, aromatic 2-aminophenylphosphonate residue in P1 position of the inhibitor was designed. The target compound was synthesised starting from diethyl 2-nitrophosphonate in several step procedure. The decrease in basicity of the terminal amino moiety of the modified analogue in fact resulted in satisfactory improvement of hydrolytic stability of the P–N bo…

PharmacologyModels MolecularMagnetic Resonance SpectroscopyChemistryStereochemistryphosphonamidateLAP inhibitorsOrganic ChemistryGeneral MedicineAminopeptidaseChemical synthesisResidue (chemistry)HydrolysisLeucyl AminopeptidaseOrganophosphorus CompoundsDrug StabilityDrug DesignDrug Discoveryhydrolytic stabilityMoietyChemical stabilityProtease InhibitorsLeucineLeucyl aminopeptidaseEuropean journal of medicinal chemistry
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