期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 7, 页码 2425-2430出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1312976111
关键词
alpha-hemolysin; beta-barrel; lipid reorganization; nanopore
资金
- National Institutes of Health
- European Commission
- Oxford Nanopore Technologies
- European Research Council
- Biotechnology and Biological Sciences Research Council
- Felix Scholarship
- Engineering and Physical Sciences Research Council
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.
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