Layer-by-Layer Assembly of Supported Lipid Bilayer Poly-l-Lysine Multilayers

Heath, George R., Li, Mengqiu, Polignano, Isabelle L., Richens, Joanna, Catucci, Gianluca, O'Shea, Paul, Sadeghi, Sheila J., Gilardi, Gianfranco, Butt, Julea and Jeuken, Lars J. C. (2016) Layer-by-Layer Assembly of Supported Lipid Bilayer Poly-l-Lysine Multilayers. Biomacromolecules, 17 (1). pp. 324-335. ISSN 1525-7797

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    Abstract

    Multilayer lipid membranes perform many important functions in biology, such as electrical isolation (myelination of axons), increased surface area for biocatalytic purposes (thylakoid grana and mitochondrial cristae), and sequential processing (golgi cisternae). Here we develop a simple layer-by-layer methodology to form lipid multilayers via vesicle rupture onto existing supported lipid bilayers (SLBs) using poly l-lysine (PLL) as an electrostatic polymer linker. The assembly process was monitored at the macroscale by quartz crystal microbalance with dissipation (QCM-D) and the nanoscale by atomic force microscopy (AFM) for up to six lipid bilayers. By varying buffer pH and PLL chain length, we show that longer chains (≥300 kDa) at pH 9.0 form thicker polymer supported multilayers, while at low pH and shorter length PLL, we create close packed layers (average lipid bilayers separations of 2.8 and 0.8 nm, respectively). Fluorescence recovery after photobleaching (FRAP) and AFM were used to show that the diffusion of lipid and three different membrane proteins in the multilayered membranes has little dependence on lipid stack number or separation between membranes. These approaches provide a straightforward route to creating the complex membrane structures that are found throughout nature, allowing possible applications in areas such as energy production and biosensing while developing our understanding of the biological processes at play.

    Item Type: Article
    Additional Information: This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
    Faculty \ School: Faculty of Science > School of Chemistry
    Faculty of Science > School of Biological Sciences
    University of East Anglia > Faculty of Science > Research Groups > Biophysical Chemistry
    University of East Anglia > Faculty of Science > Research Groups > Molecular Microbiology
    Depositing User: Pure Connector
    Date Deposited: 02 Feb 2016 13:11
    Last Modified: 25 Jul 2018 11:44
    URI: https://ueaeprints.uea.ac.uk/id/eprint/56928
    DOI: 10.1021/acs.biomac.5b01434

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