BMAP27, a bovine cathelicidin-derived peptide, was studied by using coarse-grained (CG) molecular dynamics employing the Martini force field, which has recently been further optimized for studying protein-membrane interactions . The CG-MD study revealed that BMAP27 loses helicity when interacting with POPC membranes but not with POPG membranes, a finding that mirrors the behavior of LL-37 . The authors suggested that BMAP27 acts via a carpet-like mechanism in zwitterionic membranes (POPC) but forms toroidal pores in anionic membranes (POPG), similar to other helical-kink peptides like LL-37 .