@article { ISI:000228859400005,
	title = {Perturbation of a lipid membrane by amphipathic peptides and its role in pore formation},
	journal = {EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS},
	volume = {34},
	year = {2005},
	month = {MAY},
	pages = {230-242},
	abstract = {We study the structural and energetic consequences of (α-helical) amphipathic peptide adsorption onto a lipid membrane and the subsequent formation of a transmembrane peptide pore. Initially, each peptide binds to the membrane surface, with the hydrophobic face of its cylinder-like body inserted into the hydrocarbon core. Pore formation results from subsequent peptide crowding, oligomerization, and eventually reorientation along the membrane normal. We have theoretically analyzed three peptide-membrane association states: interfacially-adsorbed monomeric and dimeric peptides, and the multi-peptide transmembrane pore state. Our molecular-level model for the lipid bilayer is based on a combination of detailed chain packing theory and a phenomenological description of the headgroup region. We show that the membrane perturbation free energy depends critically on peptide orientation: in the transmembrane pore state the lipid perturbation energy, per peptide, is smaller than in the adsorbed state. This suggests that the gain in conformational freedom of the lipid chains is a central driving force for pore formation. We also find a weak, lipid-mediated, gain in membrane perturbation free energy upon dimerization of interfacially-adsorbed peptides. Although the results pertain mainly to weakly-charged peptides, they reveal general properties of the interaction of amphipathic peptides with lipid membranes.},
	issn = {0175-7571},
	doi = {10.1007/s00249-004-0445-9},
	author = {Zemel, A and Ben-Shaul, A and May, S}
}
