Search results for "oligopeptides"

showing 10 items of 136 documents

Synthesis, Structure and Conformation of Partially-Modified Retro- and Retro-Inversoψ[NHCH(CF3)]Gly Peptides

2003

Partially modified retro- (PMR) and retro-inverso (PMRI) psi[NHCH(CF(3))]Gly peptides, a conceptually new class of peptidomimetics, have been synthesized in wide structural diversity and variable length by aza-Michael reaction of enantiomerically pure alpha-amino esters and peptides with enantiomerically and geometrically pure N-4,4,4-trifluorocrotonoyl-oxazolidin-2-ones. The factors underlying the observed moderate to good diastereocontrol have been investigated. The conformations of model PMR-psi[NHCH(CF(3))]Gly tripeptides have been studied in solution by (1)H NMR spectroscopy supported by MD calculations, as well as in the solid-state by X-ray diffraction. Remarkable stability of turn-l…

Models MolecularMagnetic Resonance SpectroscopyMolecular StructureProtein ConformationChemistryStereochemistryHydrogen bondOrganic ChemistryTemperatureReproducibility of ResultsGeneral ChemistryTripeptideCrystal structureCrystallography X-RayBiochemistryProtein Structure SecondaryCatalysisSolutionsModels ChemicalTetrahedral carbonyl addition compoundIntramolecular forceSide chainProton NMRPeptide bondOligopeptidesChemistry - A European Journal
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Conformational and structural analysis of the equilibrium between single- and double-strand ?-helix of aD,L-alternating oligonorleucine

2004

Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called beta-helices. The major feature of these structures is that they can be associated with the transmembrane ion-conducting channel activity in some natural antibacterial peptides. The study of alternating D,L synthetic peptides is critical to understand how factors such as surrounding media, main chain length, type of side chain and terminal groups, among others, can determine the adoption of a specific kind of beta-helix. Early studies pointed out that the peptides Boc-(D-NLeu-L-NLeu)(6)-D-MeNLe-L-Nl-D-Nl-L-Nl-OMe (Boc: tert-butyloxycarb…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationStereochemistryDimerMolecular Sequence DataBiophysicsDNA Single-StrandedBeta helixStereoisomerismAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicschemistry.chemical_compoundProtein structureNorleucineSide chainAmino Acid SequenceChemistryOrganic ChemistryStereoisomerismDNAGeneral MedicineNuclear magnetic resonance spectroscopyCrystallographyNucleic Acid ConformationThermodynamicsOligopeptidesBiopolymers
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Synthesis of enantiopure pyrrolidine-derived peptidomimetics and oligo-beta-peptides via nucleophilic ring-opening of beta-lactams.

2006

The synthesis of the two enantiomers of pyrrolidine-derived spiro beta-lactams by resolution with D- and L-Boc phenylalanine is described. The potential of these optically active spiro beta-lactams on the synthesis of peptidomimetics as analogues of melanostatin is evaluated. Theoretical studies of several models, at the Becke3LYP/6-31+G* level of theory, together with previous experimental evidences from our group, gathered by NMR, allow us to design structures that can efficiently mimic some biologically active peptide-type molecules. On the other hand, the spiro beta-lactams have shown their utility in the preparation of beta-peptides. As an example, a homo-tetra-beta-peptide was synthes…

Models MolecularMagnetic Resonance SpectroscopyPyrrolidinesPeptidomimeticStereochemistryStereoisomerismRing (chemistry)beta-LactamsChemical synthesisPyrrolidinechemistry.chemical_compoundNucleophileβ lactamschemistry.chemical_classificationOrganic ChemistryMolecular MimicryStereoisomerismNuclear magnetic resonance spectroscopyGeneral MedicineMSH Release-Inhibiting HormoneAmino acidEnantiopure drugchemistryDrug DesignLactamOligopeptidesThe Journal of organic chemistry
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News from an Ancient World: Two Novel Astacin Metalloproteases from the Horseshoe Crab

2008

In this work, we report the cloning, heterologous expression, and characterization of two novel astacin proteases from the chelicerate Limulus polyphemus (horseshoe crab), designated as LAST (Limulus astacin) and LAST_MAM (Limulus astacin containing a MAM domain), respectively. The expression pattern showed ubiquitous occurrence of LAST_MAM, while LAST was predominantly restricted to the eyes and brain, indicating a function in the nervous system. Both enzymes contain the characteristic metzincin-type zinc-binding region and Met turn. While LAST is made up only of the typical prodomain and astacin-like protease domain, LAST_MAM contains an additional MAM (meprin A5 protein tyrosine phosphat…

Models MolecularProteasesDNA ComplementaryInsectaProtein familymedicine.medical_treatmentMolecular Sequence DataContext (language use)Protein tyrosine phosphataseBiologyHydroxamic AcidsNervous SystemCollagen Type IGene Expression Regulation EnzymologicCell LineEvolution MolecularStructural BiologyHorseshoe CrabsmedicineAnimalsProtein oligomerizationAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyPhylogenyExtracellular Matrix ProteinsProteaseBase SequenceCaseinsMetalloendopeptidasesbiology.organism_classificationProtein Structure TertiaryBiochemistryStructural Homology ProteinLimulusAstacinOligopeptidesProtein Processing Post-TranslationalJournal of Molecular Biology
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NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
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A molecular assembly system that renders antigens of choice highly repetitive for induction of protective B cell responses.

2002

Virus like particles (VLPs) are known to induce potent B cell responses in the absence of adjuvants. Moreover, epitope-specific antibody responses may be induced by VLPs that contain peptides inserted in their immunodominant regions. However, due to steric problems, the size of the peptides capable of being incorporated into VLPs while still permitting capsid assembly, is rather limited. While peptides genetically fused to either the N- or C-terminus of VLPs present fewer assembly problems, the immune responses obtained against such epitopes are often limited, most likely because the epitopes are not optimally exposed. In addition, such particles may be less stable in vivo. Here, we show th…

Models MolecularViral Hepatitis VaccinesHepatitis B virusMacromolecular SubstancesProtein ConformationvirusesRecombinant Fusion ProteinsProtozoan ProteinsAntigens ProtozoanBiologyProtein EngineeringEpitopePhospholipases AInclusion Bodies ViralViral Matrix ProteinsMiceImmune systemAntigenVirus-like particlemedicineAnimalsB cellB-LymphocytesMice Inbred BALB CVaccines SyntheticGeneral VeterinaryGeneral Immunology and MicrobiologyImmunodominant EpitopesImmunogenicityVaccinationPublic Health Environmental and Occupational HealthMolecular biologyHepatitis B Core AntigensPeptide FragmentsCell biologyProtein Structure TertiaryHBcAgBee VenomsInfectious Diseasesmedicine.anatomical_structureCross-Linking ReagentsCapsidDrug DesignMolecular MedicineFemaleImmunizationPeptidesOligopeptidesVaccine
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N-[tert-Butoxycarbonylglycyl-(Z)-α,β-dehydrophenylalanylglycyl-(E)-α,β-dehydrophenylalanylphenylalanyl]-4-nitroaniline ethanol solvate

2005

The alpha,beta-dehydrophenylalanine residues influence the conformation of the title pentapeptide Boc0-Gly1-Delta(Z)Phe2-Gly3-Delta(E)Phe4-L-Phe5-p-NA ethanol solvate, C42H43N7O9.C2H5OH. The first unsaturated phenylalanyl (Delta(Z)Phe2) and the third glycyl (Gly3) residues form a type I beta turn, while the second unsaturated phenylalanyl (Delta(E)Phe4) and the last phenylalanyl (L-Phe5) residues are part of a type II beta turn. All the amino acids in the peptide are linked trans to one another. The crystal structure is stabilized by intra- and intermolecular hydrogen bonds.

Models Molecularchemistry.chemical_classificationOligopeptideAniline CompoundsEthanolMolecular StructureHydrogen bondStereochemistryPeptideGeneral MedicineCrystal structureCrystallography X-RayPentapeptide repeatGeneral Biochemistry Genetics and Molecular BiologyAmino acidchemistry.chemical_compoundchemistryMoleculeOligopeptidesActa Crystallographica Section C Crystal Structure Communications
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Solution structure of aD,L-alternating oligonorleucine as a model of double-stranded antiparallel ?-helix

2002

Conformational characteristics of alternating D,L linear peptides are of particular interest because of their capacity to form transmembrane channels with different transport properties, as some natural antibiotics do. Single- and double-stranded beta-helical structures are common for alternating D,L peptides. The stability of the beta-helix depends on several structural factors, such as the backbone peptide length, type and position of side chains, and nature of terminal groups. The NMR and molecular dynamics solution conformation of a synthetic alternating D,L-oligopeptide with 15 norleucines (XVMe) has been used as a model to get insight in to the conformational features of double-strand…

Models Molecularenergy minimizationStereochemistryBiophysicsBeta helixStereoisomerismEnergy minimizationAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicsBiopolymerstwo-dimensional NMRProtein structureNorleucineSide chainDL-alternating peptNuclear Magnetic Resonance BiomolecularTransmembrane channelsChemistryOrganic ChemistryStereoisomerismGeneral Medicinemolecular dynamicsCrystallographybeta-helixOligopeptidesBiopolymers
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Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Oligopeptide assimilation and transport by Oenococcus oeni

2008

International audience; Aims: Oenococcus oeni is a slow-growing wine bacterium with a low growth yield. It thrives better on complex nitrogen sources than on free amino-acid medium. We aimed to characterize the oligopeptide use of this micro-organism. Methods and Results: Several peptides of two to eight amino-acid residues were able to provide essential amino acids. The disappearance of various peptides from extracellular medium was assessed with whole cells. Initial rates of utilization varied with the peptide, and free amino acids were released into the medium. Conclusions: Oenococcus oeni was able to transport the oligopeptides with two to five amino-acid residues tested and to hydrolys…

NitrogenWinePeptideApplied Microbiology and Biotechnology[ CHIM ] Chemical SciencesIndustrial Microbiology03 medical and health sciencesHydrolysis[CHIM]Chemical Sciences030304 developmental biologyOenococcus oeniWinechemistry.chemical_classificationBacteriological Techniques0303 health sciencesOligopeptidebiology030306 microbiologyBiological TransportGeneral MedicineMetabolismbiology.organism_classificationCulture MediaAmino acidBiochemistrychemistryAmino Acids EssentialOligopeptidesLeuconostocBacteriaBiotechnology
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