TY - JOUR
T1 - Ranatuerin 1T
T2 - An antimicrobial peptide isolated from the skin of the frog, Rana temporaria
AU - Goraya, Jadvinder
AU - Knoop, Floyd C.
AU - Conlon, J. Michael
N1 - Funding Information:
We thank Dr Sandor Lovas, Creighton University for help with secondary structure predictions, Dr Donald Babin, Creighton University for amino acid analyses, and Dr. Martina O’Flaherty, Creighton University with help with mass spectrometry. The work was supported by the National Science Foundation EPSCOR program.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1999/2
Y1 - 1999/2
N2 - 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 μM against the Gram- positive bacterium S, aureus and 40 μM against the Gram-negative bacterium Escherichia coli, but the peptide was not active against the yeast Candida albicans.
AB - 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 μM against the Gram- positive bacterium S, aureus and 40 μM against the Gram-negative bacterium Escherichia coli, but the peptide was not active against the yeast Candida albicans.
UR - http://www.scopus.com/inward/record.url?scp=0032773651&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032773651&partnerID=8YFLogxK
U2 - 10.1016/S0196-9781(98)00174-0
DO - 10.1016/S0196-9781(98)00174-0
M3 - Article
C2 - 10422869
AN - SCOPUS:0032773651
VL - 20
SP - 159
EP - 163
JO - Peptides
JF - Peptides
SN - 0196-9781
IS - 2
ER -