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 |
|---|---|
| Pages (from-to) | 159-163 |
| Number of pages | 5 |
| Journal | Peptides |
| Volume | 20 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Feb 1999 |
| Externally published | Yes |
Keywords
- Anti-microbial peptide
- Brevenin
- Esculetin
- Gaegurin
- Ranalexin
- Staphylococcus aureus
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Endocrinology
- Cellular and Molecular Neuroscience
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