Search results for "phenylalanine"

showing 10 items of 193 documents

Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.

2007

Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…

Models MolecularCircular dichroismanimal structuresMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsBiochemistryBiomaterialsResidue (chemistry)Spectroscopy Fourier Transform InfraredAlanineCrystallographyintegumentary systemChemistryMutual positionCircular DichroismOrganic ChemistryGeneral MedicineDipeptidesAmidesNMR spectra databaseSolventCrystallographyModels Chemicalembryonic structuresX-ray crystallographyBiopolymers
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Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study.

2010

Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and ty…

Models MolecularCircular dichroismanimal structuresdehydropeptide conformationMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsStereoisomerismBiochemistrydehydrophenylalanine configurationBiomaterialschemistry.chemical_compoundResidue (chemistry)Protein structureotorhinolaryngologic diseasesMoleculeAmino Acid SequencePeptide sequenceChloroformintegumentary systemMolecular StructureCircular DichroismOrganic ChemistryTemperatureStereoisomerismGeneral MedicineNuclear magnetic resonance spectroscopySolutionsnuclear magnetic resonancedehydropeptideschemistrySpectrophotometryOligopeptidesBiopolymers
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Piperazine bridged resorcinarene cages.

2010

The one-pot Mannich condensation of resorcinarenes with piperazine and an excess of formaldehyde under high dilution conditions results in a helical cage, namely, a covalently linked dimer of two resorcinarenes connected via four piperazine bridges in yields ranging from 20 to 40%. The compounds were analyzed by NMR spectroscopy, ESI mass spectrometry, and single crystal X-ray diffraction. The helical cages can encapsulate small guest molecules by adapting the cavity volume by changing the helical pitch according to the guest size.

Models MolecularDimerPhenylalanineOrganic ChemistryFormaldehydeMolecular ConformationStereoisomerismNuclear magnetic resonance spectroscopyResorcinareneCrystallography X-RayBiochemistryPiperazineschemistry.chemical_compoundPiperazinechemistryCovalent bondPolymer chemistryMoleculeOrganic chemistryPhysical and Theoretical ChemistryCalixarenesSingle crystalPiperazineOrganic letters
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alpha 11beta 1 integrin recognizes the GFOGER sequence in interstitial collagens.

2002

The integrins alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1) are referred to as a collagen receptor subgroup of the integrin family. Recently, both alpha(1)beta(1) and alpha(2)beta(1) integrins have been shown to recognize triple-helical GFOGER (where single letter amino acid nomenclature is used, O = hydroxyproline) or GFOGER-like motifs found in collagens, despite their distinct binding specificity for various collagen subtypes. In the present study we have investigated the mechanism whereby the latest member in the integrin family, alpha(11)beta(1), recognizes collagens using C2C12 cells transfected with alpha(11) cDNA and the bacterially expressed recombinant a…

Models MolecularIntegrinsDNA ComplementaryReceptors CollagenPhenylalanineIntegrinAmino Acid MotifsPlasma protein bindingBiochemistrylaw.inventionCollagen receptorMiceProtein structurelawCell AdhesionAnimalsHumansMagnesiumMolecular BiologyBinding selectivityCells Culturedchemistry.chemical_classificationbiologyDose-Response Relationship DrugCell BiologyPrecipitin TestsRecombinant ProteinsAmino acidProtein Structure TertiaryKineticschemistryBiochemistrybiology.proteinRecombinant DNACalciumCollagenPeptidesType I collagenProtein BindingThe Journal of biological chemistry
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Synthesis and structure of mono-bridged resorcinarene host: a ditopic receptor for ammonium guests.

2009

The synthesis and structural properties of tetramethoxy resorcinarene mono-crown-5 (1) are described. The binding characteristics of 1 toward acetylcholine and tetramethylammonium salts were investigated by 1H NMR titration. It was observed that the cavity of 1 provides a better fit to acetylcholine compared to the smaller tetramethylammonium cation, as acetylcholine is able to interact with both the crown ether moiety and the free hydroxyl groups of receptor 1 simultaneously.

Models MolecularMagnetic Resonance SpectroscopyStereochemistryPhenylalanineMolecular ConformationBiochemistrychemistry.chemical_compoundPolymer chemistrymedicineHydroxidesMoietyPhysical and Theoretical ChemistryCrown etherchemistry.chemical_classificationTetramethylammoniumBinding SitesOrganic ChemistryNuclear magnetic resonance spectroscopyResorcinareneCrown CompoundsQuaternary Ammonium CompoundschemistryProton NMRTitrationCalixarenesAcetylcholinemedicine.drugOrganicbiomolecular chemistry
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Phosphonic Acid Analogs of Fluorophenylalanines as Inhibitors of Human and Porcine Aminopeptidases N: Validation of the Importance of the Substitutio…

2020

International audience; A library of phosphonic acid analogs of phenylalanine substituted with fluorine, chlorine and trifluoromethyl moieties on the aromatic ring was synthesized and evaluated for inhibitory activity against human (hAPN) and porcine (pAPN) aminopeptidases. Fluorogenic screening indicated that these analogs are micromolar or submicromolar inhibitors, both enzymes being more active against hAPN. In order to better understand the mode of the action of the most active compounds, molecular modeling was used. It confirmed that aminophosphonic portion of the enzyme is bound nearly identically in the case of all the studied compounds, whereas the difference in activity results fro…

Models MolecularMolecular modelPhosphorous AcidsSwineStereochemistrylcsh:QR1-502chemistry.chemical_elementPhenylalanine[CHIM.THER]Chemical Sciences/Medicinal ChemistryCD13 AntigensRing (chemistry)Biochemistrylcsh:MicrobiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicinefluorineinhibitorsChlorineSide chainAnimalsHumansMolecular BiologyEnzyme Assays030304 developmental biologyphosphonic acid analogschemistry.chemical_classification0303 health sciencesTrifluoromethyl[CHIM.ORGA]Chemical Sciences/Organic chemistrymolecular modelingReproducibility of ResultsStereoisomerismMolecular Docking SimulationEnzymechemistry030220 oncology & carcinogenesishuman and porcine aminopeptidaseEnantiomerMolecules
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Synthesis and Inhibitory Studies of Phosphonic Acid Analogues of Homophenylalanine and Phenylalanine towards Alanyl Aminopeptidases.

2020

A library of novel phosphonic acid analogues of homophenylalanine and phenylalanine, containing fluorine and bromine atoms in the phenyl ring, have been synthesized. Their inhibitory properties against two important alanine aminopeptidases, of human (hAPN, CD13) and porcine (pAPN) origin, were evaluated. Enzymatic studies and comparison with literature data indicated the higher inhibitory potential of the homophenylalanine over phenylalanine derivatives towards both enzymes. Their inhibition constants were in the submicromolar range for hAPN and the micromolar range for pAPN, with 1-amino-3-(3-fluorophenyl) propylphosphonic acid (compound 15c) being one of the best low-molecular inhibitors …

Models MolecularProtein Conformation alpha-HelicalMolecular modelStereochemistryPhosphorous AcidsSwinePhenylalaninelcsh:QR1-502PhenylalanineCD13 Antigenscomputer-aided simulationsInhibitory postsynaptic potential01 natural sciencesBiochemistrylcsh:MicrobiologyArticlePhenylalanine derivativesSubstrate SpecificitySmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipAnimalsHumansProtein Interaction Domains and MotifsEnzyme Inhibitorsphosphonic acid inhibitorsMolecular Biology030304 developmental biologyAlaninechemistry.chemical_classification0303 health sciencesInhibitory potentialBinding Sites010405 organic chemistryChemistryAminobutyratesFluorineBromine0104 chemical sciencesIsoenzymesKineticsEnzymehuman and porcine alanine aminopeptidasefluorine and bromine substitutionThermodynamicsProtein Conformation beta-StrandProtein BindingBiomolecules
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Proteomic identification of protease cleavage sites characterizes prime and non-prime specificity of cysteine cathepsins B, L, and S.

2011

Cysteine cathepsins mediate proteome homeostasis and have pivotal functions in diseases such as cancer. To better understand substrate recognition by cathepsins B, L, and S, we applied proteomic identification of protease cleavage sites (PICS) for simultaneous profiling of prime and non-prime specificity. PICS profiling of cathepsin B endopeptidase specificity highlights strong selectivity for glycine in P3' due to an occluding loop blocking access to the primed subsites. In P1', cathepsin B has a partial preference for phenylalanine, which is not found for cathepsins L and S. Occurrence of P1' phenylalanine often coincides with aromatic residues in P2. For cathepsin L, PICS identifies 845 …

Models MolecularProteomicsTime Factorsmedicine.medical_treatmentProteolysisCathepsin LPhenylalanineGlycineBiologyBiochemistryCathepsin BPichiaCathepsin BSubstrate SpecificityCathepsin LCathepsin OPeptide LibraryCatalytic DomainmedicineHumansCathepsin SEnzyme AssaysCathepsinProteasemedicine.diagnostic_testGeneral ChemistryHydrogen-Ion ConcentrationMolecular biologyCathepsinsHEK293 CellsBiochemistryProteolysisbiology.proteinCysteinePeptide HydrolasesProtein BindingJournal of proteome research
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Ion-Pair Recognition of Tetramethylammonium Salts by Halogenated Resorcinarenes

2011

The non-covalent interactions of different upper-rim-substituted C(2)-resorcinarenes with tetramethylammonium salts were analyzed in the gas phase in an Electrospray Ionization Fourier-transform ion-cyclotron-resonance (ESI-FTICR) mass spectrometer and by (1)H NMR titrations. The order of binding strengths of the hosts towards the tetramethylammonium cation in the gas phase reflects the electronic nature of the substituents on the upper rim of the resorcinarene. In solution, however, a different trend with particularly high binding constants for halogenated resorcinarenes has been observed. This trend can be explained by a synergetic effect originating from the interaction of the halogenate…

Models MolecularSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyHalogenationPhenylalanineElectrospray ionizationInorganic chemistryMass spectrometryCatalysischemistry.chemical_compoundComputational chemistryCalixareneta116IonsTetramethylammoniumHydrogen bondOrganic ChemistryHydrogen BondingGeneral ChemistryNuclear magnetic resonance spectroscopyResorcinareneQuaternary Ammonium CompoundschemistryProton NMRSaltsCalixarenesChemistry - A European Journal
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Comparative Studies on IR, Raman, and Surface Enhanced Raman Scattering Spectroscopy of Dipeptides Containing ΔAla and ΔPhe

2012

Three dipeptides containing dehydroresidues (\DeltaAla, \Delta (Z)Phe, and \Delta (E)Phe) were examined by IR, Raman, and surface-enhanced Raman techniques for the first time. The effect of the size and isomer type of the β -substituent in the dehydroresidue on the conformational structure of the peptide was evaluated by using the analysis of IR and Raman bands. Additionally, SERS spectroscopy provided insight into the adsorption mechanism of these species on the metal surface. SERS spectra were recorded at alkaline pH on the silver sol using visible light excitation. The dehydroresidues studied here strongly influenced the SERS profile of the peptides. The most pronounced SERS signal for a…

Models MolecularSpectrophotometry InfraredSurface PropertiesPhenylalanineAnalytical chemistryMolecular ConformationSpectrum Analysis RamanVibrationMetalchemistry.chemical_compoundsymbols.namesakeAdsorptionDeprotonationSpectrophotometryMaterials ChemistrymedicineCarboxylatePhysical and Theoretical ChemistrySpectroscopyAlaninemedicine.diagnostic_testDipeptidesSurfaces Coatings and FilmsCrystallographychemistryMetalsvisual_artvisual_art.visual_art_mediumsymbolsRaman spectroscopyVisible spectrumJournal of Physical Chemistry B
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