Richard M. Epand

TL;DR: It is not likely that this diverse group of peptides has a single mechanism of action, but interaction of the peptides with membranes is an important requirement for most, if not all, antimicrobial peptides.

TL;DR: Interestingly many antimicrobial agents are polycationic and therefore likely have some effect in promoting lipid phase segregation between anionic and zwitterionic lipids, but this mechanism is expected to be most important for substances with sequential positive charges contained within a flexible molecule.

TL;DR: It is suggested that the peptide imposes positive curvature strain, facilitating the formation of a torus-type pore, and that the presence of negative curvature-inducing lipids inhibits pore formation.

TL;DR: The antimicrobial action of the ceragenins correlates better with the content of phosphatidylethanolamine in the bacterial membrane than whether or not the bacteria has an outer membrane, suggesting that the bacterial lipid composition can be an important factor in determining the sensitivity of bacteria to antimicrobial agents.

TL;DR: It is shown that random poly-β-peptide copolymers, prepared by ring-opening polymerization of β-lactams, can be tuned to display good activity against a panel of four bacteria along with low lytic activity toward human red blood cells, which support a nonclassical design hypothesis for antibacterial agents.