Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Antimicrobial Activity of Antimicrobial Peptide LPcin-YK3 Derived from Bovine Lactophoricin

  • Kim, Ji-Sun (Department of Chemistry, Hankuk University of Foreign Studies) ;
  • Jeong, Ji-Ho (Department of Chemistry, Hankuk University of Foreign Studies) ;
  • Cho, Jang-Hee (Biomaterial Research Center) ;
  • Lee, Dong-Hee (Biomaterial Research Center) ;
  • Kim, Yongae (Department of Chemistry, Hankuk University of Foreign Studies)
  • Received : 2018.05.08
  • Accepted : 2018.06.16
  • Published : 2018.08.28
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Abstract

We previously reported on lactophoricin (LPcin), a cationic ${\alpha}-helical$ antimicrobial peptide derived from bovine milk, which has antimicrobial effects on Candida albicans as well as Gram-positive and Gram-negative bacteria. In this study, we designed the LPcin-YK3 peptide, a shorter analog of LPcin, and investigated its antimicrobial activity. This peptide, consisting of 15 amino acids with + 3 net charges, was an effective antimicrobial agent against the on the Gram-positive strain, Staphylococcus aureus (MIC: $0.62{\mu}g/ml$). In addition, the hemolytic activity assay revealed that the peptide was not toxic to mouse and human erythrocytes up to $40{\mu}g/ml$. We also used circular dichroism spectroscopy to confirm that peptide in the presence of lipid has ${\alpha}-helical$ structures and later provide an overview of the relationship between each structure and antimicrobial activity. This peptide is a member of a new class of antimicrobial agents that could potentially overcome the problem of bacterial resistance caused by overuse of conventional antibiotics. Therefore, it could be used as a therapeutic or natural additive, particularly in the cosmetics industry.

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