Computational investigations of pore forming peptide assemblies in lipid bilayers.
This Letter presents the first application of a three-dimensional numerical molecular theory based modeling approach to study the structure and energetics of assemblies of peptides embedded in lipid bilayers. Coarse-grained models were used for both the peptides and lipids. Both barrel-stave and toroidal pore morphologies for the lipids near the peptide assemblies are found, but at different assembly sizes. The free energy of the assembly is found to have a global free energy minimum for a solution with a membrane-spanning toroidal pore. A pairwise approximation to this free energy is found to underpredict the free energy minimum associated with the membrane-spanning pores.
Frink
Laura J Douglas
LJ
Sandia National Laboratories, Albuquerque, New Mexico 87185, USA. ljfrink@sandia.gov
Frischknecht
Amalie L
AL
D000465:Algorithms; D001703:Biophysics / Q000379:methods; D002462:Cell Membrane / Q000378:metabolism; D019295:Computational Biology / Q000379:methods*; D008051:Lipid Bilayers / Q000737:chemistry; D008055:Lipids / Q000737:chemistry*; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000737:chemistry*; D015233:Models, Statistical; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry*; D012984:Software; D013816:Thermodynamics
D008051:Lipid Bilayers; D008055:Lipids; D008563:Membrane Lipids; D010455:Peptides