Characterization of antimicrobial peptides isolated from the skin of the Chinese frog, Rana dybowskii

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology Vol. 154; no. 2; pp. 174 - 178
• Main Authors: Jin, Li-Li, Li, Qiang, Song, Shu-Sen, Feng, Kai, Zhang, Dian-Bao, Wang, Qiu-Yu, Chen, Yu-Hua
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.10.2009
• Subjects: Amino Acid Sequence; Animals; Antimicrobial Cationic Peptides - chemistry; Antimicrobial Cationic Peptides - genetics; Antimicrobial Cationic Peptides - isolation & purification; Antimicrobial Cationic Peptides - pharmacology; Bacteria - drug effects; Biodiversity; cDNA cloning; Cloning, Molecular; DNA, Complementary - genetics; ESI-MS/MS; Freshwater; Hemolysis - drug effects; Humans; Male; Mass Spectrometry; Molecular Sequence Data; Novel antimicrobial peptides; Rana dybowskii; Ranidae; Sequence analysis; Skin - secretion; Skin secretions; cDNA cloning; ESI-MS/MS; Skin secretions; Rana dybowskii; Sequence analysis; Novel antimicrobial peptides
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/j.cbpb.2009.05.015

The skins of amphibians secrete small antimicrobial peptides that fight infection and are being explored as potential alternatives to conventional antibiotics. In this study we combined mass spectrometry with cDNA sequencing to examine antimicrobial peptides in skin secretions from the Chinese frog Rana dybowskii. Thirteen peptides having precursor sequences that resemble known antimicrobial peptides from this genus were identified, ten of which were members of previously described peptide families based on their primary structures; i.e., brevinin-1, Japonicin-1, brevinin-2 and temporin. The other three peptides from R. dybowskii, which were named dybowskin-1CDYa, dybowskin-2 CDYa and dybowskin-2CDYb, had different amino acid compositions and little sequence similarity to known antimicrobial peptides. The carboxyl terminus of dybowskin-1CDY lacked amidation and is therefore clearly distinct from temporin peptides, whereas dybowskin-2CDYa and dybowskin-2CDYb consisted of 18 amino acids and were rich in Arg residues. Chemically synthesized peptides corresponding to mature dybowskin-1CDYa and dybowskin-2CDYa had strong antimicrobial activity and caused little hemolysis of human erythrocytes, suggesting they may serve as interesting templates for the development of novel antibiotics.