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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 31, Number 9
BKCSDE 31(9)
September 20, 2010 

A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability
Jeong Kyu Bang, Yong Hai Nan, Eun Kyu Lee, Song Yub Shin*
Peptoid, Protease stability, Trp-rich model antimicrobial peptide
In order to increase protease stability of a novel Trp-rich model antimicrobial peptide, K6L2W3 (KLWKKWKKWLKNH2) and investigate the effect of L-amino acid to peptoid residue conversion on biological functions, we synthesized its antimicrobial peptoid, k6l2w3. Peptoid k6l2w3 had similar bacterial selectivity compared to peptide K6L2W3. The bactericidal rate of k6l2w3 was somewhat slower than that of K6L2W3. Peptoid k6l2w3 exhibited very little dye leakage from bacterial outer-membrane mimicking PE/PG liposomes, as observed in K6L2W3, indicating that the major target site of K6L2W3 and k6l2w3 may be not the cell membrane but the cytoplasm of bacteria. Trypsin treatment of K6L2W3 completely abolished antimicrobial activities against Escherichia coli and Staphylococcus aureus. In contrast, the antimicrobial activity of k6l2w3 was completely preserved after trypsin treatment. Taken together, our results suggested that antimicrobial peptoid k6l2w3 can potentially serves as a promising therapeutic agent for the treatment of microbial infection.
2509 - 2513
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