Three antimicrobial peptides were isolated from skin secretion of the
European frog, Rana esculenta. Two of them show similarity to brevinin
-1 and brevinin-2, respectively, two antimicrobial peptides recently i
solated from a Japanese frog [Morikawa, N., Hagiwara, K. and Nakajima,
T. (1992) Biochem. Biophys. Res. Commun. 189, 184-1901. The third one
, named esculentin, is 46 residues long and represents a different typ
e of peptide. All these peptides have as a common motif an intramolecu
lar disulfide bridge located at the COOH-terminal end. The peptides fr
om R. esculenta show distinctive antibacterial activity against repres
entative Gram-negative and Gram-positive bacterial species. In particu
lar, esculentin is the most active against Staphylococcus aureus, and
has a much lower hemolytic activity.