Peptides corresponding to helices 5 and 6 of Bax can independently form large pores of lipidic nature. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Peptides corresponding to helices 5 and 6 of Bax can independently form large pores of lipidic nature. (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1111/j.1742-4658.2006.05123.x (literal)

Alternative label

• García-Sáez A. J., Coraiola M., Dalla Serra M., Mingarro I., Muller P., Salgado J. (2006)
  Peptides corresponding to helices 5 and 6 of Bax can independently form large pores of lipidic nature.
  in The FEBS journal (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• García-Sáez A. J., Coraiola M., Dalla Serra M., Mingarro I., Muller P., Salgado J. (literal)

Pagina inizio

• 971 (literal)

Pagina fine

• 981 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 273 (literal)

Rivista

• ?The ?FEBS journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note

• FEBS Journal era precedentemente denominato European Journal of Biochemistry (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Biochemistry and Molecular Biology, University of Valencia, Spain Institute of Molecular Science, University of Valencia, Spain ITC-CNR Institute of Biophysics, Trento, Italy Institut fuer Biologie / Biophysik, Humboldt-Universita¨ t zu Berlin, Germany (literal)

Titolo

• Peptides corresponding to helices 5 and 6 of Bax can independently form large pores of lipidic nature. (literal)

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 alpha-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 redistribution of lipids, supporting a toroidal pore mechanism as in the case of the full-length protein. However, compared with the pores made by complete 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 requirements 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. (literal)

Prodotto di

• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)
• Istituto di biofisica (IBF) (Istituto)

Autore CNR

• MAURO DALLA SERRA (Unità di personale interno)
• MANUELA CORAIOLA (Unità di personale esterno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)

Autore CNR di

• MAURO DALLA SERRA (Unità di personale interno)
• MANUELA CORAIOLA (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• ?The ?FEBS journal (Rivista)