Kassinatuerin-1: A peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, kassina senegalensis

Beverly Mattute, Floyd C. Knoop, J. Michael Conlon

Research output: Contribution to journalArticle

33 Scopus citations


Kassinatuerin-1 (GFMKYIGPLI10PHAVKAISDL20I.NH2) was isolated in high yield (75 nmol/g) from an extract of the skin of a Hyperoliid frog, the African running frog Kassina senegalensis and its sequence was confirmed by total synthesis. The peptide inhibited growth of the gram-negative bacterium Escherichia coli (minimum inhibitory concentration, MIC = 4 μM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 μM), and the yeast Candida albicans (MIC = 70 μM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI10PHAVKAISDL20I.NH2) was also isolated in high yield (96 nmol/g) from the extract but was devoid of antimicrobial activity against these microrganisms. Kassinatuerin-1 may be classified with other linear, cationic antimicrobial peptides that can potentially adopt an amphipathic α-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)433-436
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Feb 16 2000


All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this