An atypical member of the brevinin-1 family of antimicrobial peptides isolated from the skin of the European frog Rana dalmatina

J. Michael Conlon, Bernhard Seidel, Per F. Nielsen

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

A single peptide with antimicrobial activity was extracted from the skin of the European agile frog (R. dalmatina). The primary structure of this 17 amino-acid-residue peptide (ILPLLLGKVVCAITKKC) does not immediately suggest membership of any of the previously described families of antimicrobial peptides from ranid frogs. However, if it is assumed that the peptide has undergone several residue deletions during the course of speciation, it shows sequence similarity with peptides belonging to the widely distributed brevinin-1 family, particularly those isolated from the related species Rana temporaria. The minimum inhibitory concentration of the peptide, termed brevinin-1Da, against the Gram-positive bacterium Staphylococcus aureus was 7 μM and against the Gram-negative bacterium Escherichia coli was 30 μM.

Original languageEnglish
Pages (from-to)191-196
Number of pages6
JournalComparative Biochemistry and Physiology - C Toxicology and Pharmacology
Volume137
Issue number2
DOIs
Publication statusPublished - Feb 2004
Externally publishedYes

Keywords

  • Antimicrobial peptide
  • Brevinin-1
  • Frog skin
  • HPLC purification
  • Temporin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Aquatic Science
  • Animal Science and Zoology
  • Toxicology
  • Cell Biology
  • Health, Toxicology and Mutagenesis

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