title: Lipid dependence of peptide-membrane interactions. Bilayer affinity and aggregation of the peptide alamethicin.
abstract: Membrane incorporation and aggregation of the peptide alamethicin have been investigated as a function of lipid type. Head group and acyl chain regions both contribute to modulate alamethicin incorporation. Specifically, the peptide prefers thin membranes and saturated chains; incorporation is reduced by the presence of cholesterol. Aggregation of the peptide in the bilayer is virtually insensitive to changes in lipid composition. These findings show some analogies to results obtained with intrinsic membrane proteins and cast doubt on the use of global membrane parameters for interpreting lipid-peptide interactions.
authors.affiliation: Biocenter, University of Basel, Switzerland.
authors.forename: S
authors.initials: S
authors.lastname: Stankowski
authors.forename: G
authors.initials: G
authors.lastname: Schwarz
mesh_terms: D000408:Alamethicin / Q000494:pharmacology*; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D002462:Cell Membrane / Q000378:metabolism; D002784:Cholesterol / Q000378:metabolism; D008051:Lipid Bilayers / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000900:Anti-Bacterial Agents; D008051:Lipid Bilayers; D000408:Alamethicin; D002784:Cholesterol