title: Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes.
abstract: Alternating amphiphilic multiblock molecules 1-4, involving fluorescent hydrophobic units, were designed as mimics for multipass transmembrane proteins. Fluorescence spectroscopy of 1-4 in liposomal membranes suggested the face-to-face stacking of the hydrophobic units to give folded structures as well as intermolecular assemblies.
authors.affiliation: Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan.
authors.forename: Takahiro
authors.initials: T
authors.lastname: Muraoka
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Shima
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Hamada
authors.forename: Masamune
authors.initials: M
authors.lastname: Morita
authors.forename: Masahiro
authors.initials: M
authors.lastname: Takagi
authors.forename: Kazushi
authors.initials: K
authors.lastname: Kinbara
mesh_terms: D001555:Benzene Derivatives / Q000138:chemical synthesis* / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D008567:Membranes, Artificial; D018716:Molecular Mimicry; D015394:Molecular Structure; D017510:Protein Folding; D013050:Spectrometry, Fluorescence
chemical_list: D001555:Benzene Derivatives; D008081:Liposomes; D008565:Membrane Proteins; D008567:Membranes, Artificial