0000000000334352

AUTHOR

Salvatore Chiantia

showing 3 related works from this author

Lipid Phase Transition in Saccharide-Coated Cholate-Containing Liposomes: Coupling to the Surrounding Matrix

2005

researchProduct

Lipid phase transition in saccharide-coated cholate-containing liposomes: coupling to the surrounding matrix.

2005

We performed FTIR measurements on cholate-containing liposomes (CCL) embedded in saccharide (trehalose or sucrose) matrixes with different contents of residual water. We obtained information on the CCL phase transition following the thermal evolution (310-70 K) of the IR spectrum of the carbonyl moieties of phospholipids in the frequency range 4225-4550 cm(-1). Furthermore, we simultaneously followed the thermal evolution of the water association band, which gave information on the behavior of the surrounding water-saccharide matrix. The analysis revealed a small sub-band of the water association band present in CCL but not in cholate-free liposomes, the thermal evolution of which is tightl…

Trehalose Liposomes Thermal behaviourSucroseSucroseSurface PropertiesLipid BilayersPhospholipidInfrared spectroscopydigestive systemPermeabilityPhase Transitionchemistry.chemical_compoundDrug Delivery Systemsstomatognathic systemHydrophilySpectroscopy Fourier Transform InfraredElectrochemistryGeneral Materials ScienceLipid bilayer phase behaviorFourier transform infrared spectroscopySpectroscopyPhospholipidsLiposomeChromatographydigestive oral and skin physiologyTemperatureTrehaloseWaterSurfaces and InterfacesCondensed Matter PhysicsTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)chemistryLiposomesCholatesHydrophobic and Hydrophilic InteractionsLangmuir : the ACS journal of surfaces and colloids
researchProduct

Pore Formation by a Bax-Derived Peptide: Effect on the Line Tension of the Membrane Probed by AFM

2007

AbstractBax is a critical regulator of physiological cell death that increases the permeability of the outer mitochondrial membrane and facilitates the release of the so-called apoptotic factors during apoptosis. The molecular mechanism of action is unknown, but it probably involves the formation of partially lipidic pores induced by Bax. To investigate the interaction of Bax with lipid membranes and the physical changes underlying the formation of Bax pores, we used an active peptide derived from helix 5 of this protein (Bax-α5) that is able to induce Bax-like pores in lipid bilayers. We report the decrease of line tension due to peptide binding both at the domain interface in phase-separa…

Models MolecularMembrane FluidityProtein ConformationLipid BilayersBiophysicsPeptide bindingPeptideMicroscopy Atomic ForceProtein structureBcl-2-associated X proteinMembrane fluiditySurface TensionComputer SimulationLipid bilayerbcl-2-Associated X Proteinchemistry.chemical_classificationLiposomeMembranesbiologyChemistryCell biologyMembraneModels ChemicalLiposomesbiology.proteinPorosityBiophysical Journal
researchProduct