Search results for "Alanine"

showing 10 items of 499 documents

Polyphasic taxonomic characterization of Lactobacillus rossiae isolates from Belgian and Italian sourdoughs reveals intraspecific heterogeneity.

2009

Abstract (GTG) 5 -PCR fingerprinting and pheS sequence analysis of 18 Lactobacillus rossiae isolates, mainly originating from Belgian and Italian artisan sourdoughs, revealed intraspecies grouping as evidenced by the delineation of three and two subgroups, respectively. On the other hand, 16S rRNA and rpoA gene sequence analysis and DNA–DNA hybridizations supported the accommodation of all isolates in a single species. No correlation between genetic and phenotypic heterogeneity was observed. Collectively, these data do not warrant taxonomic division of L. rossiae . On the other hand, the considerable differences in intraspecies sequence variation of L. rossiae isolates displayed by the pheS…

DNA BacterialRpoaSequence analysisMolecular Sequence DataBiologyApplied Microbiology and BiotechnologyMicrobiologyGenomeDNA Ribosomallaw.inventionBelgiumSpecies SpecificitylawRNA Ribosomal 16SGene(GTG)5-PCREcology Evolution Behavior and SystematicsPolymerase chain reactionGeneticsGenetic heterogeneityNucleic Acid HybridizationLactobacillus rossiae tassonomia polifasicaBreadDNA-Directed RNA PolymerasesSequence Analysis DNA16S ribosomal RNALactobacillus rossiaeDNA FingerprintingHousekeeping geneBacterial Typing TechniquesLactobacillusPhenotypeItalyGenetic markerPhesPhenylalanine-tRNA LigasePolyphasic taxonomySystematic and applied microbiology
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Key Disulfide Bonds in an Insect Hormone Binding Protein: cDNA Cloning of a Juvenile Hormone Binding Protein of Heliothis virescens and Ligand Bindin…

1995

The hemolymph juvenile hormone binding protein (JHBP) from the early fifth instar larvae of Heliothis virescens (Lepidoptera, Noctuidae) has been purified, and three cDNA clones for this protein have been isolated from a fat body cDNA library constructed in bacteriophage λZAP XR. The deduced amino acid sequence of the full-length clone predicts a mature protein consisting of 224 residues, a molecular mass of 24 976 Da, and a p/ of 5.29. Comparison of the amino acid sequence to that of the previously described JHBP from Manduca sexta shows 51 % overall identity with highly conserved N- and C-terminal regions. One of the three clones bound photoactivatable analogs of juvenile hormones with mu…

DNA ComplementaryPhotochemistryphenylalanineMolecular Sequence DataMutantcomplementary DNAMothsBiochemistryHemolymphComplementary DNAAnimalsAmino Acid SequenceDisulfidesCloning MolecularcysteinePeptide sequencehormone binding proteinhormone analogHormone binding proteinBase SequencePhotoaffinity labelingMolecular massjuvenile hormoneChemistrycDNA libraryAffinity LabelsMolecular biologyJuvenile HormonesBiochemistryLarvaJuvenile hormoneMutagenesis Site-DirectedInsect ProteinsalanineCarrier ProteinsBiochemistry
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Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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Enhanced β-turn conformational stability of tripeptides containing Δphe in cis over trans configuration

2013

Conformations of three pairs of dehydropeptides with the opposite configuration of the Delta Phe residue, Boc-Gly-Delta(Z/E)Phe-Phe-p-NA (Z- p -NA and E- p -NA), Boc-Gly-Delta(Z/E)Phe-Phe-OMe (Z-OMe and E-OMe), and Boc-Gly-Delta(Z/E)Phe-Phe-OH (Z-OH and E-OH) were compared on the basis of CD and NMR studies in MeOH, TFE, and DMSO. The CD results were used as the additional input data for the NMR-based calculations of the detailed solution conformations of the peptides. It was found that Z- p -NA, E- p -NA, Z-OMe, and Z-OH adopt the beta-turn conformations and E-OMe and E-OH are unordered. There are two overlapping type III beta-turns in Z- p -NA, type II' beta-turn in E- p -NA, and type II …

Dehydropeptide conformationCircular dichroismMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineClinical BiochemistryTripeptideCircular dichroismTemperature coefficients of amide protonsBiochemistryNuclear magnetic resonancechemistry.chemical_compoundResidue (chemistry)Trans configurationchemistry [Oligopeptides]Amideotorhinolaryngologic diseasesHydrogen bondProtein StabilityDehydropeptidesCircular DichroismOrganic ChemistryStereoisomerismchemistryIntramolecular forceddc:540Dehydrophenylalanine configurationchemical synthesis [Oligopeptides]Conformational stabilitychemistry [Phenylalanine]OligopeptidesAmino Acids
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Influence of solvents on conformation of dehydropeptides

2013

Abstract Structural investigations of dehydropeptides containing (Z)-dehydrophenylalanine in solvents characterized by different polarity are discussed. The conformational analysis are based on spectroscopic methods (NMR, CD), molecular modeling techniques and in case of the tripeptide, ab initio methods. The results of temperature experiment indicate, that the only conformation of the investigated hexapeptide 3 is stabilized by intramolecular hydrogen bonds. Depending on the length of the peptide chain, the polarity of solvent influences on arrangement of the side chain of the amino acids or of the main chain of the peptide.

Dehydropeptide conformationchemistry.chemical_classificationCircular dichroismMolecular modelDehydrophenylalanineHydrogen bondStereochemistryOrganic ChemistryAb initioPeptideTripeptideCircular dichroismSolvent polarityNMRAnalytical ChemistryInorganic ChemistrychemistryIntramolecular forceSide chainDehydropeptideSpectroscopyJournal of Molecular Structure
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Conformational analysis of α,β-dehydropeptide models at the HF and DFT levels

2004

Abstract The Ramachandran potential energy surfaces of N-acetyl-α,β-dehydroamino acid N′-monomethylamides Ac-ΔXaa-NHMe (ΔXaa=ΔAla, (Z)-ΔPhe; 1, 2) and N-acetyl-α,β-dehydroamino acid N′,N′-dimethylamides Ac-ΔXaa-NMe2 (ΔXaa=ΔAla, (Z)-ΔPhe, (Z)-ΔAbu; 3–5) were calculated at the HF/6-31G*//HF/3-21G level. The conformers localised were fully optimised at the DFT/B3LYP/6-31+G** level and their relative stabilities were analysed in terms of both π-conjugation and internal hydrogen bonding. The Ac-ΔXaa-NMe2 molecules reveal the low-energy conformer H/F, φ=−41±4°, ψ=128±4°, which is not too easily accessible for common amino acid residues. This conformer is stabilised by the bifurcated N2–CH3 O1 int…

DehydrophenylalanineHydrogen bondStereochemistryIntermolecular forceIntramolecular hydrogen bondingPotential energy surfaceCondensed Matter PhysicsDehydroalanineBiochemistryPotential energyDimethylamideschemistry.chemical_compoundchemistryDehydroalaninePotential energy surfaceMoleculePhysical and Theoretical ChemistryConformational isomerismRamachandran plotJournal of Molecular Structure: THEOCHEM
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Tuning the pH-Switch of Supramolecular Polymer Carriers for siRNA to Physiologically Relevant pH

2017

The preparation of histidine enriched dendritic peptide amphiphiles and their self-assembly into multicomponent pH-switchable supramolecular polymers is reported. Alternating histidine and phenylalanine peptide synthons allow the assembly/disassembly to be adjusted in a physiologically relevant range of pH 5.3-6.0. Coassembly of monomers equipped with dendritic tetraethylene glycol chains with monomers bearing peripheral primary amine groups leads to nanorods with a tunable cationic surface charge density. These surface functional supramolecular polycations are able to reversibly bind short interfering RNA (siRNA). The nanorod-like supramolecular polymers, their complexation with siRNA, and…

DendrimersCircular dichroismPolymers and PlasticsStereochemistryPhenylalanineStatic ElectricitySupramolecular chemistryBioengineeringPeptide02 engineering and technology010402 general chemistry01 natural sciencesPolyethylene GlycolsBiomaterialschemistry.chemical_compoundCationsAmphiphileMaterials ChemistryHistidineRNA Small Interferingchemistry.chemical_classificationDrug CarriersNanotubesGene Transfer Techniquestechnology industry and agricultureCationic polymerizationHydrogen-Ion Concentration021001 nanoscience & nanotechnologyCombinatorial chemistry0104 chemical sciencesSupramolecular polymersMonomerchemistrySelf-assemblyPeptides0210 nano-technologyBiotechnology
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Low-Q peak in X-ray patterns of choline-phenylalanine and homophenylalanine: a combined effect of chain and stacking

2016

Abstract In this contribution we report for the first time the X-ray patterns of choline-phenylalanine and choline-homophenylalanine ionic liquids. The presence of a low Q peak in both systems is another evidence that a long alkyl chain is not always needed to establish a nanodomain segregation in the liquid sufficient to be revealed by the diffraction experiment. These new data are compared with the diffraction patterns and the theoretical calculations of other choline-aminoacid ionic liquids recently reported. A significant role might be played by the stacking interactions between aromatic rings.

DiffractionChemical substancePhenylalanineStackingGeneral Physics and AstronomyPhenylalanine02 engineering and technologyIonic liquid010402 general chemistry01 natural sciencesCholinePhysics and Astronomy (all)chemistry.chemical_compoundAminoacidSettore CHIM/02Organic chemistryPhysical and Theoretical ChemistryAlkylcholine-amino acid ionic liquids EDXD; ion pairs; pre-peak; renewable materialschemistry.chemical_classificationSmall-angle X-ray scatteringSAXS; Choline; Phenylalanine; Aminoacids; Ionic liquidsAromaticitySAXS021001 nanoscience & nanotechnologyIonic liquids0104 chemical sciencesCrystallographychemistryIonic liquid0210 nano-technologyAminoacids
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Impact of the ΔPhe configuration on the Boc-Gly-ΔPhe-NHMe conformation: experiment and theory

2019

Conformational propensities of N-t-butoxycarbonyl-glycine-(E/Z)-dehydrophenylalanine N′-methylamides (Boc-Gly-(E/Z)-ΔPhe-NHMe) in chloroform were investigated by NMR and IR techniques. The low-temperature crystal structure of the E isomer was determined by single crystal X-ray diffraction and the experimental data were elaborated by theoretical calculations using DFT (B3LYP, M06-2X) and MP2 approaches. The β-turn tendencies for both isomers were determined in the gas phase and in the presence of solvent. The obtained results reveal that the configuration of ΔPhe residue significantly affects the conformations of the studied dehydropeptides. The tendency to adopt β-turn conformations is sign…

Diffractionβ-turn tendencyCrystal structure010402 general chemistry01 natural sciencesGas phaseX-ray crystal structure analysischemistry.chemical_compoundResidue (chemistry)Peptide conformational analysisZ isomer0103 physical sciencesPhysical and Theoretical Chemistry13C NMRChloroform010304 chemical physicsDehydrophenylalanineE isomer1H NMRCondensed Matter Physics0104 chemical sciencesSolventCrystallographychemistryIR spectroscopyDFT-GIAO calculationsSingle crystalStructural Chemistry
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Studies on a new potential dopaminergic agent: in vitro BBB permeability, in vivo behavioural effects and molecular docking evaluation.

2015

2-Amino-N-[2-(3,4-dihydroxy-phenyl)-ethyl]-3-phenyl-propionamide (DA-PHEN) has been previously synthesized to obtain a potential prodrug capable of release dopamine (DA) into CNS. However, DA-PHEN could act per se as a dopaminergic drug. In this study, the permeability transport (Pe), obtained by parallel artificial permeability assay (PAMPA), indicated a low passive transcellular transport (Pe = 0.32 ± 0.01 × 10(-6 )cm/s). Using the Caco-2 cell system, the Papp AP-BL in absorptive direction (3.36 ± 0.02 × 10(-5 )cm/s) was significantly higher than the Papp BL-AP in secretive direction (1.75 ± 0.07 × 10(-5 )cm/s), suggesting a polarized transport. The efflux ratio (Papp AP-BL/Papp BL-AP = 0…

DopaminePhenylalanineDopamine AgentsPharmaceutical ScienceMorris water navigation taskPharmacologyBiologyCognitive flexibilityPermeabilityIn vivoDopamineSettore BIO/10 - BiochimicaPAMPA-BBBmedicineHumansIn vivo behavioural effectDopaminergicProdrugSettore CHIM/08 - Chimica FarmaceuticaMolecular Docking SimulationSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoBlood-Brain BarrierParacellular transportMolecular docking D1-receptorSettore BIO/14 - FarmacologiaEffluxCaco-2 bidirectional assayCaco-2 CellsTranscytosisBehavioural despair testmedicine.drugJournal of drug targeting
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