Abstract
The interactions of antimicrobial peptides with model lipid bilayer membranes are discussed. The topics covered include the structures of the peptides, which are usually amphipathic; the thermodynamics of binding to the membrane surface, which include contributions from the hydrophobic effect, secondary structure formation, and electrostatic interactions; the kinetics of peptide binding and induced leakage from lipid vesicles; the molecular models proposed to describe membrane perturbation or pore formation; the nature of the pores, which may be transient and disordered; and the role of lipids in pore formation, as described by molecular dynamics and membrane elastic properties.
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