la402727a_si_001.pdf (2.32 MB)
Simulations Suggest Possible Novel Membrane Pore Structure
journal contribution
posted on 2014-02-11, 00:00 authored by Robert Vácha, Daan FrenkelAmphiphilic 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.