Defensins comprise a structural class of small cationic peptides that
exert broad-spectrum antimicrobial activities through membrane permeab
ilization. Their predominantly beta-sheet structure, stabilized by thr
ee disulfide bonds, distinguishes them from other antimicrobial peptid
es which typically form amphiphilic helices. Defensins bind to membran
es electrostatically and subsequently form apparently multimeric pores
. Recent structural and biophysical studies are beginning to provide i
nsights into the process of permeabilization.