ArticleArchives of microbiology2025
A study on antimicrobial activity of lysine-like peptoids for the development of new antimicrobials.
Article in Archives of microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The development of new medicines with unique methods of antimicrobial action is desperately needed due to the emerging multidrug-resistant bacteria, such as methicillin-resistant Staphylococcus aureus. Therefore, antimicrobial peptoids have emerged as potential new antimicrobials. Thirteen peptoid analogues have been designed and synthesized via solid phase synthesis. These peptoids have undergone a biological analysis to determine the structure-activity relationships that define their antibacterial activity. Each peptoid is composed of nine repeating N-substituted glycine monomers (9-mer). The monomer units were synthesized with three distinct alkyl side chain lengths: four-carbon butyl monomers, six-carbon hexyl monomers, and eight-carbon octyl monomers. Out of 12 different peptoids, only one peptoid called Tosyl-Octyl-Peptoid (TOP) demonstrated significant broad-spectrum bactericidal activity. TOP kills bacteria under non-dividing and dividing conditions. The Minimum Inhibitory Concentrations values of TOP for Staphylococcus epidermidis, Escherichia coli and Klebsiella were 20 µM, whereas Methicillin-resistant Staphylococcus aureus and Methicillin-sensitive Staphylococcus aureus were 40 µM. The highest MIC values were observed for Pseudomonas aeruginosa at 80 µM. The selectivity ratio was calculated, by dividing the 10% haemolysis activity (5 mM) by the median of the MIC (50 µM) yielding a selective ratio for TOP as 100. This selective ratio is well above previously reported peptidomimetics selective ratio of around 20. TOP shows broad-spectrum bactericidal action in both dividing and non-dividing bacteria in co-culture systems and intracellular bacterial killing activity. These results add new information about the antimicrobial peptoids and aid in the future design of synthetic peptoids with increased therapeutic potential.
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