Simulations suggest possible novel membrane pore structure.
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.
National Centre for Biomolecular Research, Faculty of Science and CEITEC - Central European Institute of Technology, Masaryk University , Kamenice 5, 625 00 Brno-Bohunice, Czech Republic.
Robert
R
Vácha
Daan
D
Frenkel
D016632:Apolipoprotein A-I / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry*; D008954:Models, Biological; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D016062:Porosity
D016632:Apolipoprotein A-I; D008563:Membrane Lipids; D010455:Peptides; D010743:Phospholipids