Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes.
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.
Muraoka
Takahiro
T
Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan.
Shima
Tatsuya
T
Hamada
Tsutomu
T
Morita
Masamune
M
Takagi
Masahiro
M
Kinbara
Kazushi
K
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
D001555:Benzene Derivatives; D008081:Liposomes; D008565:Membrane Proteins; D008567:Membranes, Artificial