title: Computational investigations of pore forming peptide assemblies in lipid bilayers.
abstract: 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.
authors.affiliation: Sandia National Laboratories, Albuquerque, New Mexico 87185, USA. ljfrink@sandia.gov
authors.forename: Laura J Douglas
authors.initials: LJ
authors.lastname: Frink
authors.forename: Amalie L
authors.initials: AL
authors.lastname: Frischknecht
mesh_terms: 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
chemical_list: D008051:Lipid Bilayers; D008055:Lipids; D008563:Membrane Lipids; D010455:Peptides