Search results for "Pèptids"

showing 6 items of 16 documents

The Surfactant Peptide KL4 Sequence Is Inserted with a Transmembrane Orientation into the Endoplasmic Reticulum Membrane

2008

AbstractSurfactant protein B (SP-B) is an essential component of pulmonary surfactant. Synthetic surfactant peptide KL4, a peptide based on a C-terminal amphipathic helical region of human SP-B, efficiently mimics some functional properties of SP-B and is included in therapeutic surfactant preparations used in trials to treat respiratory distress syndrome. The membrane orientation of this peptide is controversial. We used an in vitro transcription-translation system to study the insertion of hydrophobic sequences into microsomal membranes, and showed that the KL4 sequence integrates efficiently with a transmembrane orientation despite the presence of intermittent lysines throughout the sequ…

Models MolecularBiophysical LettersProtein ConformationBiophysicsBiologyEndoplasmic ReticulumCell membraneProtein structurePulmonary surfactantMembranes (Biologia)medicineAnimalsHumansPulmonary surfactant-associated protein BAmino Acid SequencePeptide sequencePulmonary Surfactant-Associated Protein BEndoplasmic reticulumCell MembraneInfant NewbornTransmembrane proteinMembranemedicine.anatomical_structureBiochemistryBiophysicsPèptidsPeptidesHydrophobic and Hydrophilic InteractionsBiophysical Journal
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Peptide Metal–Organic Frameworks for Enantioselective Separation of Chiral Drugs

2017

We report the ability of a chiral Cu(II) 3D MOF based on the tripeptide Gly-L-His-Gly (GHG) for the enantioselective separation of metamphetamine and ephedrine. Monte Carlo simulations suggest that chiral recognition is linked to preferential binding of one of the enantiomers as result of either stronger or additional H-bonds with the framework that lead to energetically more stable diastereomeric adducts. Solid phase extraction (SPE) of a racemic mixture by using Cu(GHG) as extractive phase permits isolating more than 50% of the (+)-ephedrine enantiomer as target compound in only four minutes. To the best of our knowledge, this represents the first example of a MOF capable of separating ch…

StereoisomerismTripeptideMolecular Dynamics Simulation010402 general chemistry01 natural sciencesBiochemistryCatalysisMethamphetamineColloid and Surface ChemistryOrganic chemistryMoleculeMetal-Organic FrameworksEphedrineMolecular Structure010405 organic chemistryChemistryDiastereomerEnantioselective synthesisStereoisomerismQuímicaGeneral ChemistryCombinatorial chemistry0104 chemical sciences13. Climate actionRacemic mixtureMetal-organic frameworkPèptidsEnantiomerPeptidesMonte Carlo MethodCopperJournal of the American Chemical Society
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α-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines

2004

α-Synuclein (α-syn) is a small protein of unknown function that is found aggregated in Lewy bodies, the histopathological hallmark of sporadic Parkinson disease and other synucleinopathies. Mutations in the α-syn gene and a triplication of its gene locus have been identified in early onset familial Parkinson disease. α-Syn turnover can be mediated by the proteasome pathway. A survey of published data may lead to the suggestion that overexpression of α-syn wild type, and/or their variants (A53T and A30P), may produce a decrease in proteasome activity and function, contributing to α-syn aggregation. To investigate the relationship between synuclein expression and proteasome function we have s…

Time Factorsanimal diseasesmedicine.disease_causePC12 CellsBiochemistryMicechemistry.chemical_compoundTransgenesPromoter Regions GeneticMice KnockoutGeneticsMutationInnervationBrainParkinson DiseaseProteasome complexAmyloidosisCell biologyInnervacióalpha-SynucleinAdditions and CorrectionsPèptidsPlasmidsProteasome Endopeptidase ComplexPrionsProtein subunitBlotting WesternImmunoblottingSynucleinsMice TransgenicNerve Tissue ProteinsBiologyTransfectionBacterial ProteinsMultienzyme ComplexesmedicineAnimalsImmunoprecipitationMolecular BiologyAlpha-synucleinSynucleinopathiesEpilepsyWild typeGenetic VariationCell BiologyAxonsRatsnervous system diseasesMice Inbred C57BLEpilèpsiaDisease Models AnimalLuminescent ProteinschemistryProteasomenervous systemSinapsiMutationSynapsesSynucleinAmiloïdosiPeptides
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Calcium-dependent conformational changes of membrane-bound Ebola fusion peptide drive vesicle fusion

2003

AbstractThe fusogenic subdomain of the Ebola virus envelope glycoprotein is an internal sequence located ca. 20 residues downstream the N-terminus of the glycoprotein transmembrane subunit. Partitioning of the Ebola fusion peptide into membranes containing phosphatidylinositol in the absence of Ca2+ stabilizes an α-helical conformation, and gives rise to vesicle efflux but not vesicle fusion. In the presence of millimolar Ca2+ the membrane-bound peptide adopts an extended β-structure, and induces inter-vesicle mixing of lipids. The peptide conformational polymorphism may be related to the flexibility of the virus–cell intermembrane fusogenic complex.

Vesicle fusionEbola glycoproteinSpectrophotometry InfraredProtein ConformationvirusesBiophysicsPeptideBiologymedicine.disease_causePhosphatidylinositolsBiochemistryMembrane FusionProtein Structure Secondarychemistry.chemical_compoundProtein structureFusion peptideMembranes (Biologia)Structural BiologyGeneticsmedicinePhosphatidylinositolMolecular Biologychemistry.chemical_classificationEbola virusVesicleCircular DichroismLipid bilayer fusionViral fusionWaterMembranes ArtificialCell BiologyEbolavirusLipidsTransmembrane proteinPeptide FragmentsBiochemistrychemistryLiposomesBiophysicsCalciumPèptidsPeptide–lipid interactionViral Fusion Proteins
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Peptide metal-organic frameworks under pressure: flexible linkers for cooperative compression

2018

We investigate the structural response of a dense peptide metal-organic framework using in situ powder and single-crystal X-ray diffraction under high-pressures. Crystals of Zn(GlyTyr)2 show a reversible compression by 13% in volume at 4 GPa that is facilitated by the ability of the peptidic linker to act as a flexible string for a cooperative response of the structure to strain. This structural transformation is controlled by changes to the conformation of the peptide, which enables a bond rearrangement in the coordination sphere of the metal and changes to the strength and directionality of the supramolecular interactions specific to the side chain groups in the dipeptide sequence. Compar…

chemistry.chemical_classificationDipeptideCoordination sphereSupramolecular chemistryQuímica organometàl·licaPeptideSequence (biology)02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciences0104 chemical sciencesInorganic ChemistryCrystallographychemistry.chemical_compoundchemistrySide chainMetal-organic frameworkPèptids0210 nano-technologyLinker
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