Search results for "oligopeptides"

showing 10 items of 136 documents

Pseudopeptidic ligands: exploring the self-assembly of isophthaloylbisglycine (H2IBG) and divalent metal ions.

2012

We present a systematic study of the complexation of the new pseudopeptidic ligand isophthaloylbisglycine (H(2)IBG) with divalent metal ions of varying ionic radius. This work represents the initial employment of H(2)IBG in the coordination chemistry of alkaline earth, 3d transition, Zn(II) and Cd(II) metal elements. Infrared, NMR, thermal, magnetic, adsorption and theoretical studies of these compounds are also discussed.

chemistry.chemical_classificationAlkaline earth metalIonic radiusMagnetic Resonance SpectroscopySpectrophotometry InfraredInfraredLigandChemistryInorganic chemistryGlycineMolecular ConformationLigandsCoordination complexInorganic ChemistryMetalAdsorptionX-Ray DiffractionCoordination ComplexesMetalsDivalent metal ionsvisual_artvisual_art.visual_art_mediumQD0146ta116OligopeptidesDalton transactions (Cambridge, England : 2003)
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Capillary electrochromatography analysis of hormonal cyclic and linear peptides.

2001

The retention behavior of linear and cyclic peptides has been studied by capillary electrochromatography (CEC) with a variety of different n-alkyl silica reversed-phase sorbents and also with mixed-mode phases containing both strong cation-exchange (sulfonic acid) and n-alkyl groups bonded onto the silica surface, using eluents ranging from pH 2.0 to pH 5.0. Depending upon the amino acid sequence, electrochromatographic retention of the peptides was strongly affected by the composition of the eluent, its pH value, and the choice of sorbent packed into the capillaries. The dominant separation processes operating with these charged analytes could be modulated inter alia by the content of orga…

chemistry.chemical_classificationCapillary electrochromatographyChromatographySilicon dioxideSulfonic acidSilicon DioxidePeptides CyclicCyclic peptideHormonesAnalytical Chemistrychemistry.chemical_compoundColumn chromatographyCapillary electrophoresischemistryElectrochromatographyAcetonitrileOligopeptidesChromatography Micellar Electrokinetic CapillaryAnalytical chemistry
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Conformational characteristics of homo-oligopeptides of O-benzyl-L-tyrosine+

1983

Conformational studies of X[-L-Tyr(Bzl)-]n-series bound to polyethyleneglycol (X = H2, Nps; n = 3-8) in the solid state and in solvents of different polarities and capabilities of forming hydrogen bonds are reported. By using i.r. absorption, the occurrence of the beta-structure in the higher oligomers in the solid state was established. By means of i.r. absorption and CD the onset of that ordered conformation in solution was assessed as a function of chain length. The effects induced by the presence of the N-protecting group and added base, and by changing the nature of solvent on the conformational preferences of the [-L-Tyr(Bzl)-]n homo-peptides were also examined. The 2-nitrophenylsulph…

chemistry.chemical_classificationCircular dichroismChemical PhenomenaSpectrophotometry InfraredBase (chemistry)Protein ConformationStereochemistryHydrogen bondCircular DichroismInfrared spectroscopyBiochemistryPeptide ConformationSolutionsSolventChemistrychemistry.chemical_compoundchemistryTyrosineAbsorption (chemistry)OligopeptidesDerivative (chemistry)International Journal of Peptide and Protein Research
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High yield recombinant production of a self-assembling polycationic peptide for silica biomineralization.

2015

We report the recombinant bacterial expression and purification at high yields of a polycationic oligopeptide, P5S3. The sequence of P5S3 was inspired by a diatom silaffin, a silica precipitating peptide. Like its native model, P5S3 exhibits silica biomineralizing activity, but furthermore has unusual self-assembling properties. P5S3 is efficiently expressed in Escherichia coli as fusion with ketosteroid isomerase (KSI), which causes deposition in inclusion bodies. After breaking the fusion by cyanogen bromide reaction, P5S3 was purified by cation exchange chromatography, taking advantage of the exceptionally high content of basic amino acids. The numerous cationic charges do not prevent, b…

chemistry.chemical_classificationDiatomsOligopeptideIon chromatographyPeptideIsomerasemedicine.disease_causeSilicon DioxideRecombinant Proteinslaw.inventionchemistry.chemical_compoundchemistryBiochemistrylawmedicineRecombinant DNAEscherichia coliCyanogen bromideEscherichia coliOligopeptidesBiotechnologyBiomineralizationProtein expression and purification
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Amino acid sequence and homology modeling of obtustatin, a novel non-RGD-containing short disintegrin isolated from the venom of Vipera lebetina obtu…

2003

Disintegrins represent a group of cysteine-rich peptides occurring in Crotalidae and Viperidae snake venoms, and are potent antagonists of several integrin receptors. A novel disintegrin, obtustatin, was isolated from the venom of the Vipera lebetina obtusa viper, and represents the first potent and selective inhibitor of the binding of integrin alpha(1)beta(1) to collagen IV. The primary structure of obtustatin contains 41 amino acids and is the shortest disintegrin described to date. Obtustatin shares the pattern of cysteines of other short disintegrins. However, in contrast to known short disintegrins, the integrin-binding loop of obtustatin is two residues shorter and does not express t…

chemistry.chemical_classificationModels MolecularbiologyDisintegrinsMolecular Sequence DataProtein primary structureVenomViper VenomsViper VenomsBiochemistryAmino acidBiochemistrychemistryViperidaebiology.animalFor the RecordDisintegrinbiology.proteinViperidaeAnimalsHomology modelingAmino Acid SequenceMolecular BiologyPeptide sequenceOligopeptides
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Two penta­de­hydro­peptides with different configurations of the ΔPhe residues

2009

Comparison of the crystal structures of two pentadehydropeptides containing DeltaPhe residues, namely (Z,Z)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(Z)Phe(2)-Gly(3)-Delta(Z)Phe(4)-Gly(5)-OH) methanol solvate, C(29)H(33)N(5)O(8) x CH(4)O, (I), and (E,E)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(E)Phe(2)-Gly(3)-Delta(E)Phe(4)-Gly(5)-OH), C(29)H(33)N(5)O(8), (II), indicates that the Delta(Z)Phe residue is a more effective inducer of folded structures than the Delta(E)Phe residue. The values of the torsion angles phi and psi show the presence of two …

chemistry.chemical_classificationMolecular StructureProtein ConformationOrganic CompoundsStereochemistryHydrogen bondPhenylalanineMolecular Sequence DataHydrogen BondingPhenylalanineGeneral MedicineCrystal structureCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyAmino acidCrystallographyResidue (chemistry)Protein structurechemistryIntramolecular forceMoleculeAmino Acid SequenceOligopeptidesProtein BindingActa Crystallographica Section C-Crystal Structure Communications
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Conformation of tert-butoxycarbonylglycyl-dehydroalanyl-glycine methyl ester in the crystalline state and calculated in the gas phase.

2006

tert-Butoxy­carbonyl­glycyl-dehydro­alanyl-glycine methyl ester (systematic name: methyl {2-[(tert-butoxycarbonylamino)­acetamido]prop-2-enamido}acetate) (Boc0-Gly1-ΔAla2-Gly3-OMe), C13H21N3O6, has been structurally characterized by single-crystal X-ray diffraction and by density functional theory (DFT) calculations at the B3LYP/6–311+G** level. The peptide chain in both the solid-state and calculated structures adopts neither β nor γ turns. All amino acid residues in the tripeptide sequence are linked trans to each other. The bond lengths and valence angles of the amino acid units in the crystal structure and gas phase are comparable. However, the conformation of the third glycyl residue (…

chemistry.chemical_classificationValence (chemistry)ChemistryStereochemistryMolecular ConformationGeneral MedicineCrystal structureTripeptideGeneral Biochemistry Genetics and Molecular BiologyAmino acidBond lengthCrystallographyResidue (chemistry)X-Ray DiffractionX-ray crystallographyDensity functional theoryGasesCrystallizationPeptidesOligopeptidesActa crystallographica. Section C, Crystal structure communications
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In vivo discovery of a peptide that prevents CUG-RNA hairpin formation and reverses RNA toxicity in myotonic dystrophy models

2011

6 pages, 5 figures. PMID:21730182[PubMed] PMCID: PMC3141925[Available on 2012/1/19]

congenital hereditary and neonatal diseases and abnormalitiesProtein ConformationRNA-binding proteinProtein Serine-Threonine KinasesBiologyMyotonic dystrophyMyotonin-Protein Kinasedrug discoveryMicechemistry.chemical_compoundnon-coding RNA diseasePeptide Librarymedicinal chemistryDrug DiscoveryGene expressionmedicineAnimalsMyotonic DystrophyMBNL1MultidisciplinaryMusclesdisease modelAlternative splicingRNA-Binding ProteinsRNADystrophyBiological Sciencesmedicine.diseaseRNA secondary structureMolecular biologyDNA-Binding ProteinschemistryRNA splicingDrosophilaTrinucleotide Repeat ExpansionOligopeptides
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Modular Small Diameter Vascular Grafts with Bioactive Functionalities.

2015

We report the fabrication of a novel type of artificial small diameter blood vessels, termed biomimetic tissue-engineered blood vessels (bTEBV), with a modular composition. They are composed of a hydrogel scaffold consisting of two negatively charged natural polymers, alginate and a modified chitosan, N,O-carboxymethyl chitosan (N,O-CMC). Into this biologically inert scaffold two biofunctionally active biopolymers are embedded, inorganic polyphosphate (polyP) and silica, as well as gelatin which exposes the cell recognition signal, Arg-Gly-Asp (RGD). These materials can be hardened by exposure to Ca(2+) through formation of Ca(2+) bridges between the polyanions, alginate, N,O-CMC, and polyP…

food.ingredientAlginateslcsh:MedicineBiocompatible Materialsmacromolecular substancesengineering.materialGelatinChitosanchemistry.chemical_compoundCalcium ChloridefoodTissue engineeringGlucuronic AcidBlood vessel prosthesisPolyphosphatesElastic ModulusTensile StrengthAbsorbable ImplantsMaterials TestingHuman Umbilical Vein Endothelial CellsHumanslcsh:ScienceBlood CoagulationCell Line Transformedchemistry.chemical_classificationChitosanMultidisciplinaryTissue EngineeringTissue ScaffoldsHexuronic Acidslcsh:Rtechnology industry and agricultureBiomaterialEndothelial CellsHydrogelsPolymerSilicon DioxideBlood Vessel ProsthesischemistrySelf-healing hydrogelsengineeringlcsh:QVascular GraftingBiopolymerOligopeptidesBiomedical engineeringResearch ArticlePloS one
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Activities of angiotensin-converting enzymes ACE1 and ACE2 and inhibition by bioactive peptides in porcine ocular tissues.

2009

An active local renin-angiotensin system (RAS) has recently been found in the human eye. The aim of the present study was to compare the activities of central RAS enzymes (ACE1 and 2) in porcine ocular tissues, morphologically and physiologically close to the human eye. In addition, the effects of three ACE-inhibitory tripeptides on these enzymes were evaluated.Enucleated fresh porcine eyes were used. Activities of ACE1 and ACE2 and their inhibition by bioactive tripeptides (Ile-Pro-Pro, Val-Pro-Pro, Leu-Pro-Pro) as well as by a standard ACE-inhibitor captopril were assayed in the vitreous body, the retina and the ciliary body using fluorometric detection methods.Activity of ACE1 as well as…

medicine.medical_specialtyCaptoprilgenetic structuresSwinePeptideAngiotensin-Converting Enzyme InhibitorsTripeptideBiologyIn Vitro TechniquesPeptidyl-Dipeptidase ARetina03 medical and health sciences0302 clinical medicineCiliary bodyInternal medicineRenin–angiotensin systemmedicineAnimalsPharmacology (medical)030304 developmental biologyPharmacologychemistry.chemical_classification0303 health sciencesOligopeptideRetinaCiliary Bodyeye diseases3. Good healthVitreous BodyOphthalmologyEnzymeEndocrinologymedicine.anatomical_structurechemistryAngiotensin-converting enzyme 2030221 ophthalmology & optometrysense organsAngiotensin-Converting Enzyme 2OligopeptidesJournal of ocular pharmacology and therapeutics : the official journal of the Association for Ocular Pharmacology and Therapeutics
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