M. Simmaco et al., TEMPORINS, ANTIMICROBIAL PEPTIDES FROM THE EUROPEAN RED FROG RANA-TEMPORARIA, European journal of biochemistry, 242(3), 1996, pp. 788-792
A cDNA library from the skin of Rana temporaria has been screened usin
g a cDNA fragment probe that encodes the signal peptide of the precurs
or of esculentin from the skin secretion of Rana esculenta. With this
approach, the cDNAs encoding the precursors of three peptides were iso
lated. Subsequently, the peptides predicted from the sequence of the c
loned cDNAs as well as several structurally related peptides could be
isolated from the skin secretion of R. temporaria. These peptides, whi
ch were named temporins, have a length of 10-13 residues and show some
sequence similarity to hemolytic peptides isolated from Vespa venom [
Argiolas, A. & Pisano, J. J. (1984) J. Biol. Chem. 259, 10106-10111].
Natural and synthetic temporins have antibacterial activity against gr
am-positive bacteria, but they are not hemolytic. Temporins are the sm
allest antibacterial peptides hitherto found in nature.