Isolation and characterization of novel antimicrobial peptides, rugosins A, B and C, from the skin of the frog, Rana rugosa.
Three antimicrobial peptides were isolated from the skin of Rana rugosa. The major component, designated rugosin A, consisted of 33 amino acid residues and had structural homology (45%) with brevinin-2 of Rana porosa brevipoda. This peptide strongly inhibited the growth of gram-positive bacteria (e.g. Staphylococcus aureus 209P). The second peptide (rugosin B), a minor component, also had 33 amino acid residues, but was less homologous (33%) with brevinin-2. This peptide exhibited a striking antimicrobial activity against both gram-negative (e.g., Escherichia coli NIHJ) and gram-positive bacterial species. The third one, named rugosin C, composed of 37 amino acid residues, exhibited an antimicrobial activity against gram-positive bacteria. All three peptides had an intramolecular disulfide bond at the C-terminus.
Suzuki
S
S
Department of Molecular Physiology, School of Medicine, Gunma University, Maebashi, Japan.
Ohe
Y
Y
Okubo
T
T
Kakegawa
T
T
Tatemoto
K
K
D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides; D004926:Escherichia coli / Q000187:drug effects; D006094:Gram-Positive Bacteria / Q000187:drug effects; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D011898:Ranidae; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000737:chemistry*
D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C094554:rugosin A peptide, Rana rugosa; C094555:rugosin B peptide, Rana rugosa; C094557:rugosin C peptide, Rana rugosa; C078414:brevinin-2, Rana