Richard M. Epand

TL;DR: It is demonstrated that phosphatidylcholine with (16:1)9 acyl chains undergoes polymorphic rearrangements in mixtures with 0.6-0.8 mol fraction cholesterol, and the formation of highly curved bilayer structures, such as those required for membrane fusion, can occur in mixture of cholesterol with certain phosphatids that do not form non-lamellar structures in the absence of cholesterol.

TL;DR: The molecular basis for preferential interaction with gel state lipid is suggested to be the ability of proteins to self-associate, probably at defect sites, below the phase transition temperature and thereby increase protein-protein interactions while maintaining protein-lipid and lipid-lipids interactions.

TL;DR: Lobosomes are useful tools to identify the mechanism of action of antimicrobial peptides, and they provide a simple system to complement cell studies for optimization of the potency and specificity of these agents.

TL;DR: A number of analogues of this peptide hormone with deletions in the carboxyl terminus of this putative amphipathic helix have hypocalcemic activity in vivo in rats, comparable to the native hormone, except for des-Leu19-salmon calcitonin, which is about twice as active as the unmodified hormone.

TL;DR: It is suggested that this enhanced activity is a consequence of the altered lipid interaction of +6RPTH, combined with increased conformational flexibility, particularly in the carboxyl-terminal region of the molecule.