A follow-up study by the same authors investigated PGLa dimerization, showing that PGLa has a low propensity for homodimerization. Instead, it preferentially forms heterodimers with Magainin-2, another amphibian-derived AMP . Both experimental and computational studies agree that Magainin-2 and PGLa have distinct roles in pore formation in the bacterial membrane: Magainin-2 plays a stabilizing role in the pore structure, inserting shallowly into the membrane with a large tilt angle from the membrane normal, while PGLa inserts nearly parallel to the membrane normal, with a much smaller tilt angle (Figure C) .