Lovisa Ringstad

TL;DR: This brief review aims at providing some illustrative examples on the interaction between amphiphilic peptides and phospholipid membranes an area of significant current interest focusing on antimicrobial peptides.

TL;DR: Proteolysis studies showed that LL‐37 was fully protected against enzymatic attacks while associated with the cubosomes, also denoting strong association of the peptide to the particles.

TL;DR: End-tagging by hydrophobic amino acid stretches may be employed to enhance bactericidal potency also of ultra-short AMPs at maintained limited toxicity, and facilitates straightforward synthesis of hydrophobically modified AMPs without the need for post-peptide synthesis modifications.

TL;DR: Observations of the liposome z potential at different peptide additions as well as a comparison between the results for zwitterionic and anionic liposomes suggest that electrostatically affected local packing effects are crucial for the action of these peptides, although pore formation such as that observed for many AMPs cannot be excluded at present.

TL;DR: The cubosomes were found to protect LL-37 from proteolytic degradation, resulting in a significantly better bactericidal effect after being subjected to elastase, compared to unformulated peptide.