Details

Autor(en) / Beteiligte

• Lee, Joon Ha
• Kim, In-Woo
• Kim, Mi-Ae
• Yun, Eun-Young
• Nam, Sung-Hee
• Ahn, Mi-Young
• Lee, Young Bo
• Hwang, Jae Sam

Titel

Scolopendrasin I: a novel antimicrobial peptide isolated from the centipede Scolopendra subspinipes mutilans

Ist Teil von

• International Journal of Industrial Entomology, 2015-09, Vol.31 (1), p.14-19

Ort / Verlag

한국잠사학회

Erscheinungsjahr

2015

Quelle

EZB Electronic Journals Library

Beschreibungen/Notizen

• In a previous report, we identified several candidate antimicrobial peptides through de novo RNA sequencing of the centipede Scolopendra subspinipes mutilans . Here, we identify and characterize one of these peptides, Scolopendrasin I. We identified the centipede antimicrobial peptide Cecropin from the centipede transcriptome using an SVM algorithm, and subsequently analyzed the amino acid sequence for predicted secondary structure using a GOR algorithm. We identified an alpha helical region of Cecropin and named it Scolopendrasin I. We then assessed antimicrobial and hemolytic activity of Scolopendrasin I. Scolopendrasin I showed antimicrobial activity against various microbes, including antibiotic-resistant Gram-negative bacteria, in a radial diffusion assay. Scolopendrasin I had potent antibacterial activity against acne-associated microbes in a colony count assay and showed no hemolytic activity in a hemolysis assay. In addition, we confirmed that Scolopendrasin I bound to the surface of bacteria via a specific interaction with lipoteichoic acid and lipopolysaccharide, two components of bacterial cell membranes. In conclusion, the results presented here provide evidence that this is an efficient strategy for antimicrobial peptide candidate identification and that Scolopendrasin I has potential for successful antibiotic development.