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Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores

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Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores

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	Müller, Peter
dc.contributor.author	Salgado Benito, Jesús
dc.date.accessioned	2018-04-13T14:00:58Z
dc.date.available	2018-04-13T14:00:58Z
dc.date.issued	2006
dc.identifier.citation	García-Sáez, Ana Jesús Coraiola, Manuela Dalla Serra, Mauro Mingarro Muñoz, Ismael Müller, Peter Salgado Benito, Jesús 2006 Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores Febs Journal 273 5 971 981
dc.identifier.uri	http://hdl.handle.net/10550/65662
dc.description.abstract	Proteins of the B-cell lymphoma protein 2 (Bcl2) family are key regulators of the apoptotic cascade, controlling the release of apoptotic factors from the mitochondrial intermembrane space. A helical hairpin found in the core of water-soluble folds of these proteins has been reported to be the pore- forming domain. Here we show that peptides including any of the two a-helix fragments of the hairpin of Bcl2 associated protein X (Bax) can independently induce release of large labelled dextrans from synthetic lipid vesicles. The permeability promoted by these peptides is influenced by intrinsic monolayer curvature and accompanied by fast transbilayer redis- tribution of lipids, supporting a toroidal pore mechanism as in the case of the full-length protein. However, compared with the pores made by com- plete Bax, the pores made by the Bax peptides are smaller and do not need the concerted action of tBid. These data indicate that the sequences of both fragments of the hairpin contain the principal physicochemical require- ments for pore formation, showing a parallel between the permeabilization mechanism of a complex regulated protein system, such as Bax, and the much simpler pore-forming antibiotic peptides.
dc.language.iso	eng
dc.relation.ispartof	Febs Journal, 2006, vol. 273, num. 5, p. 971-981
dc.subject	Pèptids
dc.subject	Proteïnes de membrana
dc.title	Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
dc.type	journal article	es_ES
dc.date.updated	2018-04-13T14:00:58Z
dc.identifier.doi	10.1111/j.1742-4658.2006.05123.x
dc.identifier.idgrec	025365
dc.rights.accessRights	open access	es_ES