Ranatuerin 1T: An antimicrobial peptide isolated from the skin of the frog, Rana temporaria

Jadvinder Goraya, Floyd C. Knoop, J. Michael Conlon

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22 Citations (Scopus)

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 languageEnglish
Pages (from-to)159-163
Number of pages5
JournalPeptides
Volume20
Issue number2
DOIs
Publication statusPublished (in print/issue) - Feb 1999

Funding

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.

FundersFunder number
National Science Foundation

    Keywords

    • Anti-microbial peptide
    • Brevenin
    • Esculetin
    • Gaegurin
    • Ranalexin
    • Staphylococcus aureus

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