Simulations Suggest Possible Novel Membrane Pore Structure
| Authors | |
|---|---|
| Year of publication | 2014 |
| Type | Article in Periodical |
| Magazine / Source | Langmuir |
| MU Faculty or unit | |
| Citation | |
| Web | http://pubs.acs.org/doi/abs/10.1021/la402727a |
| Doi | http://dx.doi.org/10.1021/la402727a |
| Field | Physical chemistry and theoretical chemistry |
| Keywords | MOLECULAR-DYNAMICS SIMULATIONS; ANTIMICROBIAL PEPTIDES; STATE NMR; BILAYER-MEMBRANES; LIPID-BILAYERS; AMYLOID PORES; ION CHANNELS; FORCE-FIELD; MODEL; DISEASE |
| Description | 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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