Simulations Suggest Possible Novel Membrane Pore Structure
Robert Vácha
Daan Frenkel
10.1021/la402727a.s003
https://acs.figshare.com/articles/media/Simulations_Suggest_Possible_Novel_Membrane_Pore_Structure/2324377
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.
2014-02-11 00:00:00
MARTINI force field
metastable pores
microsecond time scale
peptide
formation
membrane plane
simulations show
membrane pore
Possible Novel Membrane Pore StructureAmphiphilic proteins
toroidal pores