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Functional truncated membrane pores

Stoddart, D., Ayub, M., Hoefler, L., Raychaudhuri, P., Klingelhoefer, J. W., Maglia, G., Heron, A. & Bayley, H., 18-Feb-2014, In : Proceedings of the National Academy of Science of the United States of America. 111, 7, p. 2425-2430 6 p.

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DOI

  • David Stoddart
  • Mariam Ayub
  • Lajos Hoefler
  • Pinky Raychaudhuri
  • Jochen W Klingelhoefer
  • Giovanni Maglia
  • Andrew Heron
  • Hagan Bayley
Membrane proteins are generally divided into two classes. Integral proteins span the lipid bilayer, and peripheral proteins are located at the membrane surface. Here, we provide evidence for membrane proteins of a third class that stabilize lipid pores, most probably as toroidal structures. We examined mutants of the staphylococcal alpha-hemolysin pore so severely truncated that the protein cannot span a bilayer. Nonetheless, the doughnut-like structures elicited well-defined transmembrane ionic currents by inducing pore formation in the underlying lipids. The formation of lipid pores, produced here by a structurally defined protein, is supported by the lipid and voltage dependences of pore formation, and by molecular dynamics simulations. We discuss the role of stabilized lipid pores in amyloid disease, the action of antimicrobial peptides, and the assembly of the membrane-attack complexes of the immune system.
Original languageEnglish
Pages (from-to)2425-2430
Number of pages6
JournalProceedings of the National Academy of Science of the United States of America
Volume111
Issue number7
Publication statusPublished - 18-Feb-2014

    Keywords

  • alpha-hemolysine, beta-barrel, lipid reorganization, nanopore

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