Protein containing lipid bilayers intercalated with size-matched mesoporous silica thin films

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Protein containing lipid bilayers intercalated with size-matched mesoporous silica thin films

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Publication Article, peer reviewed scientific
Title Protein containing lipid bilayers intercalated with size-matched mesoporous silica thin films
Author Isaksson, Simon ; Watkins, Erik B. ; Browning, Kathryn L. ; Lind, Tania Kjellerup ; Cárdenas, Marité ; Hedfalk, Kristina ; Höök, Fredrik ; Andersson, Martin
Research Centre Biofilms - Research Center for Biointerfaces
Date 2017
English abstract
Proteins are key components in a multitude of biological processes, of which the functions carried out by transmembrane (membrane-spanning) proteins are especially demanding for investigations. This is because this class of protein needs to be incorporated into a lipid bilayer representing its native environment, and in addition, many experimental conditions also require a solid support for stabilization and analytical purposes. The solid support substrate may, however, limit the protein functionality due to protein–material interactions and a lack of physical space. We have in this work tailored the pore size and pore ordering of a mesoporous silica thin film to match the native cell-membrane arrangement of the transmembrane protein human aquaporin 4 (hAQP4). Using neutron reflectivity (NR), we provide evidence of how substrate pores host the bulky water-soluble domain of hAQP4, which is shown to extend 7.2 nm into the pores of the substrate. Complementary surface analytical tools, including quartz crystal microbalance with dissipation monitoring (QCM-D) and fluorescence microscopy, revealed successful protein-containing supported lipid bilayer (pSLB) formation on mesoporous silica substrates, whereas pSLB formation was hampered on nonporous silica. Additionally, electron microscopy (TEM and SEM), light scattering (DLS and stopped-flow), and small-angle X-ray scattering (SAXS) were employed to provide a comprehensive characterization of this novel hybrid organic–inorganic interface, the tailoring of which is likely to be generally applicable to improve the function and stability of a broad range of membrane proteins containing water-soluble domains.
DOI https://doi.org/10.1021/acs.nanolett.6b04493 (link to publisher's fulltext.)
Publisher American Chemical Society
Host/Issue Nanoletters;1
Volume 17
ISSN 1530-6984
Pages 476-485
Language eng (iso)
Subject Aquaporin
Lipid bilayer
Liposome
Membrane protein
Neutron reflectivity
Silica
Sciences
Research Subject Categories::NATURAL SCIENCES
Handle http://hdl.handle.net/2043/24204 Permalink to this page
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