PylA/PglA (peptide glycine-leucine-amide) precursor of 64 aas and 1 TMS.  3-d structures and simulations have revealed the overall structure, helix orientations, and tilt angles in the homo- and hetero-multimeric pores (Pino-Angeles et al. 2016).  The pore forms stable heterooligomers with magainin 2 (TC# 1.C.16.1.1) in which PglA, rather than magainin 2, forms the pore (Strandberg et al. 2016).  This occurs at lower concentrations of the two peptides than is required for each peptide to form homomeric pores.  Ulmschneider 2017 suggested that cationic antimicrobial peptides (AMPs) such as PGLa translocate across hydrophobic lipid bilayers without formation of peptide-lined channels, explaining why they induce membrane leakage and antimicrobial activity. PGLa spontaneously translocates across the membrane individually on a timescale of tens of microseconds, without forming pores. Instead, short-lived water bridges, with two or three peptides connecting at their termini, may allow both ion translocation and lipid flip-flop via a brushlike mechanism usually involving the C terminus of one peptide (Ulmschneider 2017). Another study suggested that PGLa translocates across the bilayer before membrane permeation (Parvez et al. 2018).