Development
of antimicrobial peptide (AMP)-functionalized materials
has renewed interest in using poly(ethylene glycol) (PEG)-mediated
linking to minimize unwanted interactions while engendering the peptides
with sufficient flexibility and freedom of movement to interact with
the targeted cell types. While PEG-based linkers have been used in
many AMP-based materials, the role of the tether length has been minimally
explored. Here, we assess the impact of varying the length of PEG-based
linkers on the binding of bacterial cells by surface-immobilized AMPs.
While higher surface densities of immobilized AMPs were observed using
shorter PEG linkers, the increased density was insufficient to fully
account for the increased binding activity of peptides. Furthermore,
effects were specific to both the peptide and cell type tested. These
results suggest that simple alterations in linking strategiessuch
as changing tether lengthmay result in large differences in
the surface properties of the immobilized AMPs that are not easily
predictable