PNNL

Abstract

Piscidins are the first amphipathic, cationic, antimicrobial peptides (ACAPs) to be found in the mast cells of fish, and they are believed to play a crucial role in the fight against many aquatic infections.1 Many ACAPs have been characterized functionally, and some models for their mechanism of action exist, including the barrel-stave model, the wormhole model, the carpet mechanism, and the intracellular activation of fatal pathways.2-9 Much information remains to be learned about the details of their structure, initial interactions with membranes, and the ultimate mechanism for disrupting cellular function. To this end, we employed solid-state NMR (ssNMR) to probe the structure and topology of isotopically labeled piscidins in the membrane-bound state.