Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films
Abstract
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 »
- Authors:
-
- 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)
- Publication Date:
- Research Org.:
- Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)
- Sponsoring Org.:
- Universities/Institutions; USDOE
- OSTI Identifier:
- 1418770
- Report Number(s):
- LA-UR-17-28188
Journal ID: ISSN 1530-6984; TRN: US1801299
- Grant/Contract Number:
- AC52-06NA25396
- Resource 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
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; lipids aquaporin silica; Aquaporin; Lipid bilayer; Liposome; Membrane protein; Neutron reflectivity; Silica
Citation Formats
Isaksson, Simon, Watkins, Erik Benjamin, Browning, Kathryn L., Lind, Tania Kjellerup, Cardenas, Marite, Hedfalk, Kristina, Hook, Fredrik, and Andersson, Martin. Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films. United States: N. p., 2016.
Web. doi:10.1021/acs.nanolett.6b04493.
Isaksson, Simon, Watkins, Erik Benjamin, Browning, Kathryn L., Lind, Tania Kjellerup, Cardenas, Marite, Hedfalk, Kristina, Hook, Fredrik, & Andersson, Martin. Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films. United States. https://doi.org/10.1021/acs.nanolett.6b04493
Isaksson, Simon, Watkins, Erik Benjamin, Browning, Kathryn L., Lind, Tania Kjellerup, Cardenas, Marite, Hedfalk, Kristina, Hook, Fredrik, and Andersson, Martin. Wed .
"Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films". United States. https://doi.org/10.1021/acs.nanolett.6b04493. https://www.osti.gov/servlets/purl/1418770.
@article{osti_1418770,
title = {Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films},
author = {Isaksson, Simon and Watkins, Erik Benjamin and Browning, Kathryn L. and Lind, Tania Kjellerup and Cardenas, Marite and Hedfalk, Kristina and Hook, Fredrik and Andersson, Martin},
abstractNote = {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.},
doi = {10.1021/acs.nanolett.6b04493},
journal = {Nano Letters},
number = 1,
volume = 17,
place = {United States},
year = {Wed Nov 23 00:00:00 EST 2016},
month = {Wed Nov 23 00:00:00 EST 2016}
}
Web of Science
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