A family of acyclic brevinin-1 peptides from the skin of the Ryukyu brown frog Rana okinavana

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2005-02, Vol.26 (2), p.185-190
• Main Authors: Conlon, J. Michael, Sonnevend, Agnes, Jouenne, Thierry, Coquet, Laurent, Cosquer, David, Vaudry, Hubert, Iwamuro, Shawichi
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amphibian Proteins; Animals; Anti-Bacterial Agents - chemistry; Anti-Bacterial Agents - isolation & purification; Anti-Bacterial Agents - pharmacology; Antimicrobial; Antimicrobial Cationic Peptides; Biological and medical sciences; Brevinin-1; Cysteine - chemistry; Escherichia coli - drug effects; Female; Frog skin; Fundamental and applied biological sciences. Psychology; Life Sciences; Microbial Sensitivity Tests; Molecular Sequence Data; Molecular Weight; Peptides - chemistry; Peptides - isolation & purification; Peptides - pharmacology; Proteins - chemistry; Ranatuerin-2; Ranidae; Skin - chemistry; Staphylococcus aureus - drug effects; Tissue Extracts - chemistry; Tissue Extracts - isolation & purification; Vertebrates: endocrinology
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2004.08.008

The 24 amino-acid residue antimicrobial peptide, brevinin-1 is synthesized in the skins of a wide range of species of Eurasian and North American frogs belonging to the genus Rana. All previously characterized brevinin-1 peptides contain the cyclic heptapeptide domain Cys 18-(Xaa) 4-Lys-Cys 24 at the COOH-terminus of the molecule. Four structurally related peptides were isolated from an extract of the skin of the Ryukyu brown frog Rana okinavana. The amino acid sequences of the peptides [Phe-(Xaa) 4-Ile-(Xaa) 2-Leu-Ala-Lys-Gly-Leu-Pro-Ser-Leu-Ile-Xaa-Leu-Xaa-Lys-Lys·NH 2] identified them as members of the brevinin-1 family that lacked the COOH-terminal cyclic domain but contained a C-terminally α-amidated residue. It is suggested, as one possibility, that the Cys 18 in the brevinin-1 consensus sequence has been deleted and the Cys 24 residue has mutated to a glycine that acts as substrate for peptidyl-glycine α-amidating monooxygenase. The peptides potently inhibited the growth of Escherichia coli and Staphylococcus aureus confirming that a cyclic domain is not necessary for antimicrobial activity. A fifth peptide (SFLNFFKGAA 10KNLLAAGLDK 20LKCKISGTQC 30), that also displayed broad-spectrum antimicrobial activity, was isolated from the skin extract and showed structural similarity with members of the ranatuerin-2 family previously isolated from the skin of North American ranid frogs.