Surface-immobilised antimicrobial peptoids

Abstract

Surface modification techniques that create surfaces capable of killing adherent bacteria are promising solutions to infections associated with implantable medical devices. Antimicrobial peptoid oligomers (ampetoids) that were designed to mimic helical antimicrobial peptides were synthesized with a peptoid spacer chain to allow mobility and an adhesive peptide moiety for easy and robust immobilization onto substrates. TiO 2 substrates were modified with the ampetoids and subsequently backfilled with an antifouling polypeptoid polymer in order to create polymer surface coatings composed of both antimicrobial (active) and antifouling (passive) peptoid functionalities. Confocal microscopy images show that the membranes of adherent E. coli were damaged after 2 h exposure to the modified substrates, suggesting that ampetoids retain antimicrobial properties even when immobilized onto substrates.

Covalent immobilization of antimicrobial peptides (AMPs) onto biomaterial surfaces

“…fully synthetic peptides. These are distinct from those in nature, with simpler but rationally engineered composition, obtained by varying the amino acid content and sequence and overall peptide length to achieve enhanced activity and very low cytotoxic properties [57]. For example, Mietzner and co-workers [58][59][60][61] have developed a series of de novo peptides based on structure-function properties observed in natural AMPs.…”

A review of immobilized antimicrobial agents and methods for testing

“…63 As mimics can be found for virtually any peptide function, it is not surprising that some mimics have been identified for antimicrobial functionality. Statz and coworkers 65 examined the impact that surface bound peptide mimetics have on E. coli adhesion. In that study, the authors immobilized three different peptoid sequences to titania substrates: an antimicrobial peptoid, an antihemolysis/antifouling peptoid, and a filler peptoid.…”

Peptoids for biomaterials science

“…45 Last but not least, the flexibility in peptoid synthesis enables convenient functionalization of antifouling peptoid biointerfaces, as demonstrated by peptoid brushes decorated with saccharides 46 and antimicrobial peptides. 41 …”

“…35,[40][41][42][43] Several peptoid sidechains and chain lengths have been investigated. Intriguingly, polymer brushes composed of sarcosine, the peptoid with the simplest sidechain (a single methylene: Figure 4), exhibited antifouling performance that is similarly excellent as peptoids with methoxyethyl sidechains that resemble the repeating unit of PEG.…”