Search results for "LAP inhibitors"

showing 3 items of 3 documents

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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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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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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