Simulations suggest possible novel membrane pore structure
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
24059441
DOI
10.1021/la402727a
Knihovny.cz E-resources
- MeSH
- Apolipoprotein A-I chemistry MeSH
- Models, Biological MeSH
- Phospholipids chemistry MeSH
- Membrane Lipids chemistry MeSH
- Peptides chemistry MeSH
- Porosity MeSH
- Molecular Dynamics Simulation * MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Apolipoprotein A-I MeSH
- Phospholipids MeSH
- Membrane Lipids MeSH
- Peptides MeSH
Amphiphilic proteins and peptides can induce the formation of stable and metastable pores in membranes. Using coarse-grained simulations, we have studied the factors that affect structure of peptide-stabilized pores. Our simulations are able to reproduce the formation of the well-known barrel-stave or toroidal pores, but in addition, we find evidence for a novel "double-belt" pore structure: in this structure the peptides that coat the membrane pore are oriented parallel to the membrane plane. To check the predictions of our coarse-grained model, we have performed more detailed simulations, using the MARTINI force field. These simulations show that the double-belt structure is stable up to at least the microsecond time scale.
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