Kassinatuerin-1: a peptide with broad-spectrum antimicrobial activity isolated from the skin of the hyperoliid frog, Kassina senegalensis.
Kassinatuerin-1 (GFMKYIGPLI(10)PHAVKAISDL(20)I.NH(2)) 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 microM), the gram-positive bacterium Staphylococcus aureus (MIC = 8 microM), and the yeast Candida albicans (MIC = 70 microM). A structurally related peptide, kassinatuerin-2 (FIQYLAPLI(10)PHAVKAISDL(20)I.NH(2)) 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 alpha-helical conformation but it contains almost no amino acid sequence identity with previously characterized bioactive peptides from frog skin.
Mattute
B
B
Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178, USA.
Knoop
F C
FC
Conlon
J M
JM
D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001001:Anura; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology; D011506:Proteins / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000737:chemistry*; D013211:Staphylococcus aureus / Q000187:drug effects
D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D010455:Peptides; D011506:Proteins; C404848:kassinatuerin-1