Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability

  • Bang, Jeong-Kyu (Division of Magnetic Resonance, Korea Basic Science Institute) ;
  • Nan, Yong-Hai (Department of Bio-Materials, Graduate School, and Department of Cellular & Molecular Medicine, School of Medicine, Chosun University) ;
  • Lee, Eun-Kyu (Department of Bio-Materials, Graduate School, and Department of Cellular & Molecular Medicine, School of Medicine, Chosun University) ;
  • Shin, Song-Yub (Department of Bio-Materials, Graduate School, and Department of Cellular & Molecular Medicine, School of Medicine, Chosun University)
  • Received : 2010.07.01
  • Accepted : 2010.07.12
  • Published : 2010.09.20
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Abstract

In order to increase protease stability of a novel Trp-rich model antimicrobial peptide, $K_6L_2W_3$ (KLWKKWKKWLK-$NH_2$)and investigate the effect of L-amino acid to peptoid residue conversion on biological functions, we synthesized its antimicrobial peptoid, $k_6l_2w_3$. Peptoid $k_6l_2w_3$ had similar bacterial selectivity compared to peptide $k_66L_2W_3$. The bactericidal rate of $k_6l_2w_3$ was somewhat slower than that of $K_6L_2W_3$. Peptoid $k_6l_2w_3$ exhibited very little dye leakage from bacterial outer-membrane mimicking PE/PG liposomes, as observed in $K_6L_2W_3$, indicating that the major target site of $K_6L_2W_3$ and $k_6l_2w_3$ may be not the cell membrane but the cytoplasm of bacteria. Trypsin treatment of $K_6L_2W_3$ completely abolished antimicrobial activities against Escherichia coli and Staphylococcus aureus. In contrast, the antimicrobial activity of $k_6l_2w_3$ was completely preserved after trypsin treatment. Taken together, our results suggested that antimicrobial peptoid $k_6l_2w_3$ can potentially serves as a promising therapeutic agent for the treatment of microbial infection.

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