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Title: Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films

Here, 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 amore » 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.« less
Authors:
 [1] ; ORCiD logo [2] ;  [3] ;  [4] ;  [4] ;  [5] ;  [6] ; ORCiD logo [1]
  1. Chambers Univ. of Technology, Gothenburg (Sweden)
  2. Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
  3. Uppsala Univ., Uppsala (Sweden)
  4. Malmo Univ., Malmo (Sweden)
  5. Univ. of Gothenburg, Gothenburg (Sweden)
  6. Chalmers Univ. of Technology, Gothenburg (Sweden)
Publication Date:
Report Number(s):
LA-UR-17-28188
Journal ID: ISSN 1530-6984; TRN: US1801299
Grant/Contract Number:
AC52-06NA25396
Type:
Accepted Manuscript
Journal Name:
Nano Letters
Additional Journal Information:
Journal Volume: 17; Journal Issue: 1; Journal ID: ISSN 1530-6984
Publisher:
American Chemical Society
Research Org:
Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
Sponsoring Org:
Universities/Institutions; USDOE
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; lipids aquaporin silica; Aquaporin; Lipid bilayer; Liposome; Membrane protein; Neutron reflectivity; Silica
OSTI Identifier:
1418770