0000000001194622

AUTHOR

Gianfranco Menestrina

showing 1 related works from this author

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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