Richard M. Epand

TL;DR: It is suggested that in addition to binding to the enzyme, the acyl chain at the sn‐1 position may contribute to the depth of insertion of the DAG into the membrane.

TL;DR: Differential scanning calorimetry, 2H nuclear magnetic resonance (NMR), and 13C NMR of phosphatidylcholine bilayers in the presence of Z-D-P he-L-PheGly indicate that this hydrophobic peptide penetrates the phospholipid bilayer but does not strongly perturb the properties of phosph atidyl choline bilayer with a large effective radius of curvature.

TL;DR: It is determined that replacing cholesterol with its enantiomer, ent-cholesterol, alters the modulation of lipid organization by peptides, and a specific chirality of membrane lipids is required for peptide-induced formation of cholesterol-rich domains.

TL;DR: It is shown that Ac-hE18A-NH2, a dual-domain cationic apolipoprotein-mimetic peptide, reduces plasma cholesterol levels in dyslipidemic mice and has stronger interactions with lipids than did m18L.

TL;DR: The results demonstrate that having the carbobenzoxy group on the amino-terminus of fFG is important for giving the peptide derivative the property of inhibiting membrane fusion.