Richard M. Epand

TL;DR: A major advance in the concept of the fluid mosaic model of biological membranes in recent years has been the appreciation of the domain structure of membranes, which is now well developed with mammalian plasma membranes but is an emerging focus with regard to bacterial membranes.

TL;DR: This study provides further understanding of why α/β-peptide II is more toxic to micro-organisms with a high PE content in their membrane as well as for the lack of toxicity of α/ β- peptide I with these cells, emphasizing the potential importance of the lipid composition of the cell surface in determining selective toxicity of anti-microbial agents.

TL;DR: Two magainin analogues with enhanced hydrophobicity are designed and interactions with lipid bilayers and biological activities were examined, demonstrating that the hydrophobia of the peptide also controls the mode of action and is dependent on the position of thehydrophobic amino acids in the peptides sequence.

TL;DR: The membrane-permeabilizing efficiency of analogs with enhanced angle of positively charged residues is reduced due to electrostatic repulsion between adjacent helices within the pore, thus resulting in a decreased pore-forming probability and/or pore destabilization.

TL;DR: This review discusses three of the more extensively studied forms of this enzyme, DGKalpha, DGkvarepsilon, and DGKzeta, which have an important role in immune function and its activity is modulated by several mechanisms.