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Biophys. J. BioFAST: First Published April 6, 2007. doi:10.1529/biophysj.106.100370
© 2007 by the Biophysical Society.

A more recent version of this article appeared on July 1, 2007.
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MEMBRANES

Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM

Ana J. García-Sáez 1, Salvatore Chiantia 1, Jesus Salgado 2 and Petra Schwille 1*

1 TU Dresden
2 Univesitat de Valencia

* To whom correspondence should be addressed. E-mail: petra.schwille{at}biotec.tu-dresden.de.

Submitted on November 2, 2006
Revised on December 27, 2006
Accepted on 21 February 2007


  Abstract
Bax 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-{alpha}5) 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-separated lipid bilayers and at the pore edge in AFM film-rupture experiments. Such a decrease in line tension may be a general strategy of pore-forming peptides and proteins, as it affects the energetics of the pore and stabilizes the open state.

Key Words: Bcl-2 family of proteins, apoptosis, supported bilayer, toroidal pore




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Copyright © 2007 by the Biophysical Society.