Simulations suggest possible novel membrane pore structure
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
24059441
DOI
10.1021/la402727a
Knihovny.cz E-zdroje
- MeSH
- apolipoprotein A-I chemie MeSH
- biologické modely MeSH
- fosfolipidy chemie MeSH
- membránové lipidy chemie MeSH
- peptidy chemie MeSH
- poréznost MeSH
- simulace molekulární dynamiky * MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- apolipoprotein A-I MeSH
- fosfolipidy MeSH
- membránové lipidy MeSH
- peptidy 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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