S. Thennarasu et R. Nagaraj, Synthetic peptides corresponding to the beta-hairpin loop of rabbit defensin NP-2 show antimicrobial activity, BIOC BIOP R, 254(2), 1999, pp. 281-283
Citations number
26
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Mammalian defensins, a class of antibacterial peptides, are composed of 29-
35 amino acids with six cysteines which form three disulfide bonds. Structu
ral studies indicate a triple stranded beta-sheet structure with a well def
ined beta-hairpin loop at the C-terminal region. It is demonstrated in this
report that 18 and 26 residue synthetic peptides corresponding to the beta
-hairpin region, constrained by a single disulfide bond, have potent antimi
crobial activity without hemolytic activity, Circular dichroism spectroscop
y indicates that the single S-S bridge appears to constrain the peptides to
a beta-structure. Peptides corresponding to the beta-hairpin region of def
ensins could thus be attractive candidates as therapeutic agents as well as
good model compounds for investigation of the various physiological action
s of defensins, (C) 1999 Academic Press.