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 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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 159-163 |
| Number of pages | 5 |
| Journal | Peptides |
| Volume | 20 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1 1999 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Endocrinology
- Physiology
- Cellular and Molecular Neuroscience
Cite this
Ranatuerin 1T : An antimicrobial peptide isolated from the skin of the frog, Rana temporaria. / Goraya, Jadvinder; Knoop, Floyd C.; Conlon, J. Michael.
In: Peptides, Vol. 20, No. 2, 01.02.1999, p. 159-163.Research output: Contribution to journal › Article
}
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
PY - 1999/2/1
Y1 - 1999/2/1
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
VL - 20
SP - 159
EP - 163
JO - Peptides
JF - Peptides
SN - 0196-9781
IS - 2
ER -