A family of kassinatuerin-2 related peptides from the skin secretion of the African hyperoliid frog, Kassina maculata.

Lei Wang, Tianbao Chen, Mei Zhou, Stephanie McGrath, Brian Walker, Christopher Shaw, Sean Gorman

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

We describe the isolation and structural characterization of a family of antimicrobial peptides related to kassinatuerin-2, from the skin secretion of the African hyperoliid frog, Kassina maculata. All four peptides, designated kassinatuerin-2Ma through Md, are C-terminally-amidated 20-mers with the consensus sequence – FX1GAIAAALPHVIX2AIKNAL – where X1 = L/F/V/I and X2 = S/N. All four peptides are encoded by precursors of 69 amino acids. Synthetic replicates of all kassinatuerin-2 related peptides displayed a potent inhibitory activity against Staphylococcus aureus with a minimal inhibitory concentration of 16 µM, at which concentration, however, they effected 18% haemolysis of horse erythrocytes after 2 h. Despite obvious membranolytic properties, all peptides were ineffective at inhibiting the growth of Escherichia coli at concentrations up to 200 µM and were relatively ineffective against Candida albicans (MIC 120 µM). The kassinatuerin-2 related peptides of K. maculata skin secretion thus possess a discrete antimicrobial and weak haemolytic activity in contrast to the prototype kassinatuerin-2 from the skin secretion of Kassina senegalensis.
Original languageEnglish
Pages (from-to)1428-1433
Number of pages6
JournalPeptides
Volume30
Issue number8
DOIs
Publication statusPublished - Aug 2009

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Cellular and Molecular Neuroscience

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