High in vitro antimicrobial activity of β-peptoid–peptide hybrid oligomers against planktonic and biofilm cultures of Staphylococcus epidermidis

Strategies employed in the design and optimization of synthetic antimicrobial peptide amphiphiles with enhanced therapeutic potentials

“…In the study by Barron's group, a library of rationally designed amphiphilic helical peptoids were demonstrated to have low-micromolar antibacterial activities similar to that mediated by pexiganan and melittin and that the antimicrobial trends in relation to structure and amphipathicity follow closely to that observed with conventional AMPs [122]. In addition, the combination of β-peptoids with α-amino acids has also been demonstrated to be an effective strategy to obtain unique hybrid structures that are protease resistant and with promising antimicrobial activities and selectivities [125][126][127].…”

The proteolytically stable peptidomimetic Pam-(Lys-βNSpe)6-NH2 selectively inhibits human neutrophil activation via formyl peptide receptor 2

“…To circumvent these problems, we and others have developed synthetic HDP mimics with improved characteristics such as increased protease resistance [43][44][45]. Stable HDP mimics based on a design with alternating α-amino acids and peptoid residues (see Figure 1A) have been found to exhibit antimicrobial activity against planktonic bacteria and biofilm, and to possess antiplasmodial as well as immunomodulatory activities [43,[46][47][48][49]. The aim of the present study was to investigate the effects of lipidated peptidomimetics, belonging to the subclass of -peptide/β-peptoid hybrids, on the inflammatory responses of human neutrophils.…”

End group modification: Efficient tool for improving activity of antimicrobial peptide analogues towards Gram-positive bacteria

“…Peptide analogues with a 64 design mimicking the activity of AMPs are usually preferred over 65 sequence-modified peptides due to their superior stability towards 66 enzymatic degradation [6]. Previously, we have shown that hybrids 67 consisting of a-amino acids and a-peptoid (N-alkylated glycine) or 68 b-peptoid (N-alkylated b-alanine) residues exhibit antibacterial 69 [7,8] and antiplasmodial activity [9], significant anti-biofilm 70 [10,11] activity as well as cell-penetrating properties [12][13][14]. In 71 the present work, we show that N-terminal modification may serve 72 as an efficient tool for enhancing the activity against clinically 73 important Gram-positive pathogens.…”