Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films
Artikel i vetenskaplig tidskrift, 2017

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.

titania

Liposome

membranes

vesicle fusion

Silica

Lipid bilayer

Neutron reflectivity

conductance

Membrane protein

channel

Aquaporin

angstrom

Författare

Simon Isaksson

Chalmers, Kemi och kemiteknik, Tillämpad kemi, Teknisk ytkemi

E. B. Watkins

K. L. Browning

T. K. Lind

M. Cardenas

Kristina Hedfalk

Göteborgs universitet

Fredrik Höök

Chalmers, Fysik, Biologisk fysik

Martin Andersson

Chalmers, Kemi och kemiteknik, Tillämpad kemi, Teknisk ytkemi

Nano Letters

1530-6984 (ISSN) 1530-6992 (eISSN)

Vol. 17 1 476-485

Ämneskategorier

Fysik

Kemiteknik

Fundament

Grundläggande vetenskaper

DOI

10.1021/acs.nanolett.6b04493

PubMed

28073257

Mer information

Senast uppdaterat

2018-08-23