Antimicrobial dermcidin, DCD.  Based on 3-d structural data, dermcidin forms an architecture of high-conductance transmembrane channels, composed of zinc-connected trimers of antiparallel helix pairs. Molecular dynamics simulations elucidated the unusual membrane permeation pathway for ions and showed adjustment of the pore to various membranes (Song et al. 2013). DCD assembles in solution into a hexameric pre-channel complex before  targeting the membrane and integration, the complex follows a deviation of the barrel stave model (Zeth and Sancho-Vaello 2017). The tilt angle and the conductance is determined by the membrane thickness and the cholesterol composition (Song et al. 2019). A soluble 48 residue fragment has been structurally characterized (PDB: 2KSG_A). Membrane interactions and pore formation have been investigated for α-helical AMPs leading to the formulation of three basic mechanistic models: the barrel stave, toroidal, and carpet models. Human cathelicidin (LL-37) and dermcidin (DCD) are α-helical, and their structures have been solved at atomic resolution. DCD assembles in solution into a hexameric pre-channel complex before  actual membrane targeting and integration steps occur, and the complex follows a deviation of the barrel stave model (Zeth and Sancho-Vaello 2017).