Interaction of Indolicidin with Model Lipid Bilayers: FT-IR Spectroscopic Study

摘要

Indolicidin, a tridecapeptide amide, was isolated by Selsted et al. from the cytopiasmic granules of bovine neutrophils (its primary structure is H-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH_2). Named for its unusual abundance of tryptophan (38%), indolicidin is a structurally unique antimicrobial peptide. In this regard, much interest has been focused on its therapeutic utility. Indolicidin was found, however, to be highly toxic not only to bacterial cells but to mammalian cells as well. Nonetheless, Ahmad et al reported that liposomally encapsulated indolicidin had significantly reduced toxicity.