Yoonkyoung Park

Chosun University, Gwangju, Gwangju, South Korea

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Publications (1)1.59 Total impact

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    ABSTRACT: A novel bacterial cell-selective antimicrobial peptide, IsCT-P (ILKKIWKPIKKLF-NH(2)), was designed based on the scorpion-derived alpha-helical antimicrobial peptide, IsCT. Here, we investigated the effect of substituting Pro(8) of IsCT-P with the Ala-peptoid residue (N-methylglycine) on the peptide's structure and mechanism of action. Circular dichroism analysis revealed that the modified peptide, IsCT-a, has a much lower alpha-helicity than IsCT-P in membrane mimicking conditions, suggesting the peptoid residue provides much more structural flexibility than the proline residue. IsCT-a was also much less effective than IsCT-P at causing leakage of fluorescent dye entrapped within negatively charged vesicles and at dissipating the membrane potential of Staphylococcus aureus. Collectively, our results suggest that the antibacterial action of IsCT-a is due to the inhibition of intracellular targets rather than the disruption and depolarization of bacterial cell membranes.
    No preview · Article · Oct 2006 · Biotechnology Letters

Publication Stats

2 Citations
1.59 Total Impact Points

Top Journals


  • 2006
    • Chosun University
      • Research Center for Proteineous Materials (RCPM)
      Gwangju, Gwangju, South Korea