Difference between magainin-2 and melittin assemblies in phosphatidylcholine bilayers: results from coarse-grained simulations.
We performed coarse-grained computer simulations using MARTINI force field to study the difference in the self-assembly and possible pore creation in DPPC phospholipid membranes by two different antimicrobial peptides: magainin-2 and melittin. Simulations showed that magainin-2 peptides create large sized disordered toroidal pores that allow easy water permeation across them. Melittin assemblies contain peptides in U-shaped conformations that, although creating holes in membranes, block effectively the passage of water. These observed structures are consistent with the dye efflux experiments performed on vesicles exposed to solutions containing antimicrobial peptides.
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Kolattukudy P
KP
Santo
Max L
ML
Berkowitz
D000595:Amino Acid Sequence; D008051:Lipid Bilayers; D054806:Magainins / Q000737:chemistry*; D008555:Melitten / Q000737:chemistry*; D008969:Molecular Sequence Data; D010713:Phosphatidylcholines / Q000737:chemistry*
D008051:Lipid Bilayers; D054806:Magainins; D010713:Phosphatidylcholines; D008555:Melitten