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Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins

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Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins

dc.contributor.author	García-Sáez, Ana Jesús
dc.contributor.author	Coraiola, Manuela
dc.contributor.author	Dalla Serra, Mauro
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Menestrina, Gianfranco
dc.contributor.author	Salgado Benito, Jesús
dc.date.accessioned	2018-04-12T14:24:07Z
dc.date.available	2018-04-12T14:24:07Z
dc.date.issued	2005
dc.identifier.citation	García-Sáez, Ana Jesús Coraiola, Manuela Dalla Serra, Mauro Mingarro Muñoz, Ismael Menestrina, Gianfranco Salgado Benito, Jesús 2005 Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins Biophysical Journal 88 6 3976 3990
dc.identifier.uri	http://hdl.handle.net/10550/65614
dc.description.abstract	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 a-helix of a colicinlike hydrophobic hairpin (a-helix 5 of Bax and a-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly a-helical structures and induce the release of entrapped calcein. In planar lipid membranes they form ion conducting channels, which in the case of the Bax-derived peptide are char- acterized by a two-stage pattern, a large conductivity and lipid-charge-dependent ionic selectivity. These features, together with the influence of intrinsic lipid curvature on the poration activity and the existence of two helical stretches of different orientations for the membrane-bound peptide, suggest that it forms mixed lipidic/peptidic pores of toroidal structure. In contrast, the assayed Bid fragment shows a markedly different behavior, characterized by the formation of discrete, steplike channels in planar lipid bilayers, as expected for a peptidic pore lined by a bundle of helices.
dc.language.iso	eng
dc.relation.ispartof	Biophysical Journal, 2005, vol. 88, num. 6, p. 3976-3990
dc.subject	Pèptids
dc.subject	Proteïnes
dc.title	Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
dc.type	journal article	es_ES
dc.date.updated	2018-04-12T14:24:07Z
dc.identifier.doi	10.1529/biophysj.104.058008
dc.identifier.idgrec	011003
dc.rights.accessRights	open access	es_ES