title: Ranatuerin 1T: an antimicrobial peptide isolated from the skin of the frog, Rana temporaria.
abstract: A peptide, termed ranatuerin 1T, with growth-inhibiting activity toward Staphylococcus aureus, was isolated from an extract of the skin of the European brown frog, Rana temporaria. The primary structure of the peptide was established as: GLLSGLKKVG10 KHVAKNVAVS20LMDSLKCKIS30GDC. In common with other anti-microbial peptides from Ranid frogs, (e.g., ranalexin, ranatuerins, gaegurins, brevinins, esculetins, rugosins), ranatuerin IT contains an intramolecular disulfide bridge forming a heptapeptide ring but there is little structural similarity outside this cyclic region. The minimum inhibitory concentration (MIC) of ranatuerin 1T was 120 microM against the Gram-positive bacterium S. aureus and 40 microM against the Gram-negative bacterium Escherichia coli, but the peptide was not active against the yeast Candida albicans.
authors.affiliation: Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178, USA.
authors.forename: J
authors.initials: J
authors.lastname: Goraya
authors.forename: F C
authors.initials: FC
authors.lastname: Knoop
authors.forename: J M
authors.initials: JM
authors.lastname: Conlon
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000890:Anti-Infective Agents / Q000302:isolation & purification*; D023181:Antimicrobial Cationic Peptides; D004305:Dose-Response Relationship, Drug; D005260:Female; D008297:Male; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides; D011506:Proteins / Q000302:isolation & purification*; D011896:Rana temporaria; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000737:chemistry*
chemical_list: D029845:Amphibian Proteins; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D011506:Proteins; C121230:ranatuerin