dermaseptin-s and indolicidin

Species right across the evolutionary scale from insects to mammals use peptides as part of their host-defense system to counter microbial infection. The primary structures of a large number of these host-defense peptides have been determined. While there is no primary structure homology, the peptides are characterized by a preponderance of cationic and hydrophobic amino acids. The secondary structures of many of the host-defense peptides have been determined by a variety of techniques. The acyclic peptides tend to adopt helical conformation, especially in media of low dielectric constant, whereas peptides with more than one disulfide bridge adopt beta-structures. Detailed investigations have indicated that a majority of these host-defense peptides exert their action by permeabilizing microbial membranes. In this review, we discuss structural and charge requirements for the interaction of endogenous antimicrobial peptides and short peptides that have been derived from them, with membranes.

Topics: Amino Acid Sequence; Amphibian Proteins; Animals; Anti-Infective Agents; Antimicrobial Cationic Peptides; Cell Membrane; Cell Wall; Fish Venoms; Lipid Bilayers; Melitten; Models, Molecular; Molecular Sequence Data; Peptides; Peptides, Cyclic; Permeability; Protein Conformation; Proteins; Seminal Vesicle Secretory Proteins; Structure-Activity Relationship; Sulfhydryl Compounds