AI Article Synopsis
- Amphipathic cationic peptoids, designed as antimicrobial alternatives to peptides, are being studied for their effectiveness.
- The research investigates the use of triazolium groups in peptoid synthesis to enhance antimicrobial properties and promote helical structures.
- Findings indicate that these triazolium-based peptoids can selectively kill bacteria like E. coli and S. aureus without harming mammalian cells, likely through mechanisms like pore formation leading to cell membrane damage.
Article Abstract
Amphipathic cationic peptoids (N-substituted glycine oligomers) represent a promising class of antimicrobial peptide mimics. The aim of this study is to explore the potential of the triazolium group as a cationic moiety and helix inducer to develop potent antimicrobial helical peptoids. Herein we report the first solid-phase synthesis of peptoid oligomers incorporating 1,2,3-triazolium-type side chains and their evaluation against Escherichia coli, Enterococcus faecalis, and Staphylococcus aureus. Several triazolium-based oligomers, even of short length, selectively kill bacteria over mammalian cells. SEM visualization of S. aureus cells treated with a dodecamer and a hexamer reveals severe cell membrane damage and suggests that the longer oligomer acts by pore formation.
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| http://dx.doi.org/10.1002/cmdc.201800273 | DOI Listing |
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