Abstract
The use of hydrogels has garnered significant interest as biomaterial and drug delivery platforms for anti-infective applications. For decades antimicrobial peptides have been heralded as a much needed new class of antimicrobial drugs. Self-assembling peptide hydrogels with inherent antimicrobial ability have recently come to the fore. However, their fundamental antimicrobial properties, selectivity and mechanism of action are relatively undefined. This review attempts to establish a link between antimicrobial efficacy; the self-assembly process; peptide–membrane interactions and mechanical properties by studying several reported peptide systems: β-hairpin/β-loop peptides; multidomain peptides; amphiphilic surfactant-like peptides and ultrashort/low molecular weight peptides. We also explore their role in the formation of amyloid plaques and the potential for an infection etiology in diseases such as Alzheimer's. We look briefly at innovative methods of gel characterization. These may provide useful tools for future studies within this increasingly important field.
Highlights
There is a need for innovative antimicrobial platforms in order to successfully address growing concerns of antimicrobial resistance to conventional therapeutic approaches.[1]
This review demonstrates the promise of peptide hydrogels as future antimicrobial platforms
A major benefit of this approach is the inherent antimicrobial activity provided by the hydrogel forming peptide molecule
Summary
She is currently working as an EPSRC Research Fellow within the Biofunctional Nanomaterials group in the School of Pharmacy, Queen’s University Belfast which focuses on the design and development of self-assembling nanostructures/platforms for biomedical applications. Self-assembling peptide hydrogels are an emerging field of research for drug delivery,[15] tissue engineering,[16] cell culture and electronic applications.[17,18] The peptide motif provides the ability to tailor assembly and hydrogel formation in response to a variety of external stimuli including pH, temperature, light, ionic strength and specific enzymes.[19] The amphiphilic and hydrophobic nature of peptide’s amino acid building blocks act as drivers for self-assembly and formation of a variety of nanostructures, including nanofibers, nanotubes, nanocages, nanobelts and nanovesicles (Fig. 1) As highlighted above, such properties are central tenet to the antimicrobial activity of peptides. Review self-assembly behaviour and mechanical properties (e.g. gel strength) leading to new avenues of research for biomaterial design
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