A Short Peptide Synthesized on the Basis of Coleoptericin A from Allomyrina dichotoma Shows Similar Anti-Escherichia coli Action

Abstract

Short antimicrobial peptides were synthesized on the basis of the active site of coleoptericin A, an antimicrobial peptide from Allomyrina dichotoma. Antimicrobial assays of these peptides were tested to find a lead peptide for development of novel antimicrobial peptide. The 20-mer peptide, VGKTWIKVIRGIGKSKIKWI-NH₂, maintained anti-Escherichia coli action similar to the original coleoptericin A. Furthermore, anti-E. coli activity of the 20-mer peptide was stronger than coleoptericin A, although the original antimicrobial peptide was shorten from 72-mer to 20-mer and replaced some amino acids. These results suggest this 20-mer peptide, derived from coleoptericin A, is a good candidate as a lead peptide for development of novel antimicrobial peptide against E. coli.