International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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Antibacterial Activity of Peptides Synthesized Based on the Bombus ignitus abaecin, A Novel Proline-Rich Antimicrobial Peptide

  • Kim, Seong-Ryul (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Lee, Eun-Mi (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Yoon, Hyung-Joo (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Choi, Yong-Soo (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Yun, Eun-Young (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Hwang, Jae-Sam (Department of Agricultural Biology, National Institute of Agricultural Science & Technology) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, In-Hee (Department of Life Science, Hoseo University) ;
  • Kim, Ik-Soo (College of Agriculture and Life science, Chonnam National University)
  • Published : 2007.06.30
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Abstract

Abaecin is a largest member of the proline-rich anti-microbial peptide family found only in the hymenopterans. A cDNA of abaecin was previously isolated and cloned from Bombus ignitus: the mature peptide of Bombus ignitus abaecin was composed of 39 amino acid residues. In the present study, we determined the antibacterial effect of B. ignitus abaecin synthesized at several lengths against several bacteria by radial diffusion assay. The 37-mer peptide (Ab37) inhibited the growth of Gram-negative bacteria Escherichia coli ML-35, Pseudomonas aeruginosa and Salmonela typhimurium, but showed limited inhibitory activity toward Gram-positive bacteria, except for Micrococcus luteus. The truncated 26-mer peptide (Ab26), which was synthesized after truncating some amino acid residues at both N-terminus and C-terminus from the Ab37 peptide, still showed equivalent antibacterial activity to the Ab37. On the other hand, several further truncated peptides exhibited lower activity then did Ab37 peptide.

Keywords

References

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