title: The energetics of binding of a signal peptide to lipid bilayers: the role of bilayer properties.
abstract: The interactions between a signal peptide and a variety of lipid bilayers have been studied with direct binding assays, CD and isothermal titration calorimetry. We find that the binding of this peptide is influenced by charges and dipoles located in the bilayer interfacial region, as well as by the presence of cholesterol in the bilayer. These studies show that bilayer compositional and mechanical variations found in different biological membranes can affect the partitioning of peptides into the bilayer.
authors.affiliation: Department of Cell Biology, Duke University Medical Center, Durham, NC 27710, USA. t.mcintosh@cellbio.duke.edu
authors.forename: T J
authors.initials: TJ
authors.lastname: McIntosh
authors.forename: A
authors.initials: A
authors.lastname: Vidal
authors.forename: S A
authors.initials: SA
authors.lastname: Simon
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D008051:Lipid Bilayers / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D021382:Protein Sorting Signals / Q000502:physiology*; D013816:Thermodynamics
chemical_list: D008051:Lipid Bilayers; D010455:Peptides; D021382:Protein Sorting Signals