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Issue 1, 2011
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Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes

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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.

Graphical abstract: Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes

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Publication details

The article was received on 07 Jul 2010, accepted on 27 Aug 2010 and first published on 17 Sep 2010


Article type: Communication
DOI: 10.1039/C0CC02420A
Chem. Commun., 2011,47, 194-196

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    Mimicking multipass transmembrane proteins: synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes

    T. Muraoka, T. Shima, T. Hamada, M. Morita, M. Takagi and K. Kinbara, Chem. Commun., 2011, 47, 194
    DOI: 10.1039/C0CC02420A

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