Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii

J. M. Conlon, Á Sonnevend, M. Patel, C. Davidson, P. F. Nielsen, T. Pál, L. A. Rollins-Smith

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)

Abstract

The emergence of strains of the human pathogen Candida albicans with resistance to commonly used antibiotics has necessitated a search for new types of antifungal agents. Six peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions from the foothill yellow-legged frog Rana boylii. Brevinin-1BYa (FLPILASLAA10KFGPKLF CLV 20TKKC) was particularly potent against C. albicans [minimal inhibitory concentration (MIC) = 3 μM] and also active against Escherichia coli (MIC = 17 μM) and Staphylococcus aureus (MIC = 2 μM), but its therapeutic potential for systemic use is limited by its strong hemolytic activity (HC50 = 4 μM). The single amino acid substitution (Phe12 → Leu) in brevinin-1BYb resulted in a fourfold lower potency against C. albicans and the additional amino acid substitutions (Lys11 → Thr, Phe17 → Leu and Val20 → IIe) in brevinin-1BYc resulted in a ninefold decrease in activity. Two members of the ranatuerin-2 family and one member of the temporin family were also isolated from the secretions but showed relatively low potency against the three microorganisms tested.

Original languageEnglish
Pages (from-to)207-213
Number of pages7
JournalJournal of Peptide Research
Volume62
Issue number5
DOIs
Publication statusPublished - Nov 2003
Externally publishedYes

Keywords

  • Amphibian skin
  • Brevinin-1
  • Candida albicans
  • Rana
  • Ranatuerin-2
  • Temporin

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Fingerprint

Dive into the research topics of 'Isolation of peptides of the brevinin-1 family with potent candidacidal activity from the skin secretions of the frog Rana boylii'. Together they form a unique fingerprint.

Cite this