Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films
- Chambers Univ. of Technology, Gothenburg (Sweden)
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
- Uppsala Univ., Uppsala (Sweden)
- Malmo Univ., Malmo (Sweden)
- Univ. of Gothenburg, Gothenburg (Sweden)
- Chalmers Univ. of Technology, Gothenburg (Sweden)
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 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.
- Research Organization:
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
- Sponsoring Organization:
- Universities/Institutions; USDOE
- Grant/Contract Number:
- AC52-06NA25396
- OSTI ID:
- 1418770
- Report Number(s):
- LA-UR--17-28188
- Journal Information:
- Nano Letters, Journal Name: Nano Letters Journal Issue: 1 Vol. 17; ISSN 1530-6984
- Publisher:
- American Chemical SocietyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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