Bactrocerin-1: A novel inducible antimicrobial peptide from pupae of oriental fruit fly Bactrocera dorsalis Hendel

✍ Scribed by Xiang-Li Dang; Jin-Huan Tian; Wan-Ying Yang; Wen-Xian Wang; Jun Ishibashi; Ai Asaoka; Hui-Yu Yi; Yi-Feng Li; Yang Cao; Minoru Yamakawa; Shuo-Yang Wen

• Book ID: 101607698
• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 299 KB
• Volume: 71
• Category: Article
• ISSN: 0739-4462
• DOI: 10.1002/arch.20308

✦ Synopsis

Abstract

A novel antimicrobial peptide, Bactrocerin‐1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin‐1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin‐1 showed very high similarity to the active fragment (46V‐65S‐NH~2~) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin‐1 is a hydrophobic, positively charged, and Lys/Ile/Gly‐rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin‐1 showed a very broad spectrum of anti‐microbial activity against Gram‐positive bacteria, Gram‐negative bacteria, and fungi. Bactrocerin‐1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 µM. Analysis of the Helical‐wheel projection and the CD spectrum suggested that Bactrocerin‐1 contains the amphipathic α‐helix. © 2009 Wiley Periodicals, Inc.