Berlin 2008 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 27: Membrane Morphology and Adhesion
BP 27.5: Vortrag
Freitag, 29. Februar 2008, 11:45–12:00, C 243
Coarse-grained simulation studies of peptide-induced pore formation in lipid membranes — Gregoria Illya1,2 and •Markus Deserno2,3 — 1Institut für Anorganische und Physikalische Chemie, TU Darmstadt, Petersenstraße 20, 64287 Darmstadt — 2MPI für Polymerforschung, Ackermannweg 10, 55128 Mainz — 3Department of Physics, Carnegie Mellon University, 5000 Forbes Ave, Pittsburgh PA 15213, USA
We investigate generic aspects of the impact of antimicrobial peptides on lipid membranes using a solvent-free coarse-grained simulation technique. Lipids are modeled as strings of four beads, peptides as bead-composed cylinders with hydrophilic caps and a transmembrane hydrophobic region with possibly small hydrophilic strips. As a function of hydrophobic peptide-lipid attraction the preferred state of the peptide changes from desorbed to adsorbed to inserted, and peptides can mutually catalyze their own insertion. In the presence of hydrophilic strips along the transmembrane region peptides aggregate to form pores in the bilayer, whose size and morphology depends on the generic interaction parameters. For instance, whether pores appear as “toroidal” or “barrel stave” is triggered by the strength of an additional hydrophobic peptide-peptide cohesion beyond the hydrophilicity-driven pore formation.