A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability

作者：Bang Jeong Kyu; Nan Yong Hai; Lee Eun Kyu; Shin Song Yub^*

来源：Bulletin of the Korean Chemical Society, 2010, 31(9): 2509-2513.

DOI：10.5012/bkcs.2010.31.9.2509

• Peptoid
• Protease stability
• Trp-rich model antimicrobial peptide

In order to increase protease stability of a novel Trp-rich model antimicrobial peptide, K(6)L(2)W(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(6)l(2)w(3). Peptoid k(6)l(2)w(3) had similar bacterial selectivity compared to peptide K(6)L(2)W(3). The bactericidal rate of k(6)l(2)w(3) was somewhat slower than that of K(6)L(2)W(3). Peptoid k(6)l(2)w(3) exhibited very little dye leakage from bacterial outer-membrane mimicking PE/PG liposomes, as observed in K(6)L(2)W(3), indicating that the major target site of K(6)L(2)W(3) and k(6)l(2)w(3) may be not the cell membrane but the cytoplasm of bacteria. Trypsin treatment of K(6)L(2)W(3) completely abolished antimicrobial activities against Escherichia coli and Staphylococcus aureus. In contrast, the antimicrobial activity of k(6)l(2)w(3) was completely preserved after trypsin treatment. Taken together, our results suggested that antimicrobial peptoid k(6)l(2)w(3) can potentially serves as a promising therapeutic agent for the treatment of microbial infection.

• 出版日期2010-9-20