title: A coarse-grained model for peptide aggregation on a membrane surface.
abstract: The aggregation of peptides on a lipid bilayer is studied using coarse-grained molecular dynamics in implicit solvent. Peptides bind to and self-assemble on the membrane surface into β-rich fibrillar aggregates, even under conditions where only disordered oligomers form in bulk solution. Relative to a solid surface, the membrane surface facilitates peptide mobility and a more complex network of morphology transitions as aggregation proceeds. Additionally, final aggregate structures realized on the membrane surface are distinct from those observed on a comparable solid surface. The aggregated fibrils alter the local structure and material properties of the lipid bilayer in their immediate vicinity but have only a modest effect on the overall bending rigidity of the bilayer.
authors.affiliation: Department of Physics, University of California Santa Barbara , Santa Barbara, California 93106, United States.
authors.forename: Alex
authors.initials: A
authors.lastname: Morriss-Andrews
authors.forename: Frank L H
authors.initials: FL
authors.lastname: Brown
authors.forename: Joan-Emma
authors.initials: JE
authors.lastname: Shea
mesh_terms: D008051:Lipid Bilayers / Q000737:chemistry*; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry*
chemical_list: D008051:Lipid Bilayers; D010455:Peptides