Niv Papo

TL;DR: In the last decade intensive research has been conducted to determine the role of innate immunity host defense peptides (also termed antimicrobial peptides) in the killing of prokaryotic and eukaryotic cells as discussed by the authors.

TL;DR: It is concluded that a strong binding of a peptide to LPS aggregates accompanied by aggregate dissociation prevents LPS from binding to the carrier protein lipopolysaccharide-binding protein, or alternatively to its receptor, and hence inhibits cytokine secretion.

TL;DR: Model phospholipid membranes have been used to study the mode of action of antimicrobial peptides and it is demonstrated that peptides that act preferentially on bacteria are also able to interact with and permeate efficiently anionicospholipids, whereas peptide that lyse mammalian cells bind and permeates efficiently both acidic and zwitterionic phospholIPids membranes.

TL;DR: A 12-mer amphipathic α-helical antimicrobial peptide and its diastereomer (4D-K5L7) is synthesized and investigated, finding that although both peptides strongly bind LPS bilayers and depolarize bacterial cytoplasmic membranes, only the diastsereomer kills Gram-negative bacteria.

TL;DR: SP is used to study the interaction between lytic peptides and lipid bilayers and clearly differentiate between the two general mechanisms: pore formation by melittin only in zwitterionic membranes and a detergent-like effect for all the peptides in negatively charged membranes, in agreement with their biological function.