Search results for "Lipid-protein interaction"

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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C):Structure and surface activity

2006

  Udgivelsesdato: 2006-Apr Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich alpha helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new prepar…

BioquímicaRecombinant membrain proteinSurface PropertiesSize-exclusion chromatographyMolecular Sequence DataPhospholipidBiophysicsBiologyBiochemistrylaw.inventionchemistry.chemical_compoundAffinity chromatographyPulmonary surfactantMembranes (Biologia)lawAnimalsHumansPulmonary surfactant-associated protein CAmino Acid SequenceLipid bilayerConserved SequencePhospholipidsMammalsDrug CarriersChromatographySequence Homology Amino AcidSP-CProteïnes de membranaSurfactant protein CPulmonary surfactantCell BiologyPulmonary Surfactant-Associated Protein CRecombinant ProteinsKineticschemistryBiochemistryRecombinant DNALipid-protein interactionPeptidesSequence Alignment
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Structural characterisation of the natural membrane-bound state of melittin: a fluorescence study of a dansylated analogue

1997

Abstract The binding of a dansylated analogue of melittin (DNC–melittin) to natural membranes is described. The cytolytic peptide from honey bee venom melittin was enzymatically labelled in its glutamine-25 with the fluorescent probe monodansylcadaverine using guinea pig liver transglutaminase. The labelled peptide was characterised functionally in cytolytic assays, and spectroscopically by circular dichroism and fluorescence. The behaviour of DNC–melittin was, in all respects, indistinguishable from that of the naturally occurring peptide. We used resonance energy transfer to measure the state of aggregation of melittin on the membrane plane in synthetic and natural lipid bilayers. When bo…

Circular dichroismProtein ConformationGlutamineGuinea PigsLipid BilayersBiophysicsPeptideHemolysiscomplex mixturesBiochemistryMelittinchemistry.chemical_compoundCadaverinePhosphatidylcholineAnimalsHumansLipid bilayerFluorescent Dyeschemistry.chemical_classificationBinding SitesTransglutaminasesCircular DichroismDansyl labelingtechnology industry and agricultureMembrane structureMelittinFluorescence energy transferCell BiologyMelittenFluorescenceSpectrometry FluorescenceMembraneEnergy TransferLiverBiochemistrychemistryBiophysicslipids (amino acids peptides and proteins)Natural membraneLipid-protein interactionProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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