Membrane interactions and pore formation by the antimicrobial peptide protegrin.

ABSTRACT: Protegrin is an antimicrobial peptide with a β-hairpin structure stabilized by a pair of disulfide bonds. It has been extensively studied by solid-state NMR and computational methods. Here we use implicit membrane models to examine the binding of monomers on the surface and in the interior of the membrane, the energetics of dimerization, the binding to membrane pores, and the stability of different membrane barrel structures in pores. Our results challenge a number of conclusions based on previous experimental and theoretical work. The burial of monomers into the membrane interior is found to be unfavorable for any membrane thickness. Because of its imperfect amphipathicity, protegrin binds weakly, at most, on the surface of zwitterionic membranes. However, it binds more favorably onto tor

SUBMITTER: Lazaridis T 

PROVIDER: S-EPMC3566446 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature