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Bridging across length scales : multi-scale ordering of supported lipid bilayers via lipoprotein self-assembly and surface patterning

Vinchurkar, Madhuri S; Bricarello, Daniel A; Lagerstedt, Jens O LU ; Buban, James P; Stahlberg, Henning; Oda, Michael N.; Voss, John C LU and Parikh, Atul N (2008) In Journal of the American Chemical Society 130(33). p.9-11164
Abstract

We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase... (More)

We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase rHDL with a chemically patterned hydrophilic/hydrophobic surface produces a novel compositional pattern, caused by an increased affinity for adsorption onto hydrophilic regions relative to the surrounding hydrophobic regions. Further, by simple chemical denaturation of the boundary protein, nanoscale compartmentalization can be selectively erased, thus producing patterns of laterally fluid, lipid bilayers structured solely at the mesoscopic length scale. Since these aqueous phase microarrays of nanostructured lipid bilayers allow for membrane proteins to be embedded within single nanoscale bilayer compartments, they present a viable means of generating high-density membrane protein arrays. Such a system would permit in-depth elucidation of membrane protein structure-function relationships and the consequences of membrane compartmentalization on lipid dynamics.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Dimyristoylphosphatidylcholine, Lipid Bilayers, Lipoproteins, Models, Molecular, Nanostructures, Particle Size, Protein Array Analysis, Surface Properties, Ultraviolet Rays, Water, Journal Article, Research Support, U.S. Gov't, Non-P.H.S.
in
Journal of the American Chemical Society
volume
130
issue
33
pages
9 - 11164
publisher
The American Chemical Society
external identifiers
  • scopus:50249084457
ISSN
1520-5126
DOI
10.1021/ja803110v
language
English
LU publication?
no
id
89b8132a-cfcb-4cde-af65-76ac91f8cbfc
date added to LUP
2017-10-19 20:10:03
date last changed
2017-10-23 10:09:24
@article{89b8132a-cfcb-4cde-af65-76ac91f8cbfc,
  abstract     = {<p>We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase rHDL with a chemically patterned hydrophilic/hydrophobic surface produces a novel compositional pattern, caused by an increased affinity for adsorption onto hydrophilic regions relative to the surrounding hydrophobic regions. Further, by simple chemical denaturation of the boundary protein, nanoscale compartmentalization can be selectively erased, thus producing patterns of laterally fluid, lipid bilayers structured solely at the mesoscopic length scale. Since these aqueous phase microarrays of nanostructured lipid bilayers allow for membrane proteins to be embedded within single nanoscale bilayer compartments, they present a viable means of generating high-density membrane protein arrays. Such a system would permit in-depth elucidation of membrane protein structure-function relationships and the consequences of membrane compartmentalization on lipid dynamics.</p>},
  author       = {Vinchurkar, Madhuri S and Bricarello, Daniel A and Lagerstedt, Jens O and Buban, James P and Stahlberg, Henning and Oda, Michael N. and Voss, John C and Parikh, Atul N},
  issn         = {1520-5126},
  keyword      = {Dimyristoylphosphatidylcholine,Lipid Bilayers,Lipoproteins,Models, Molecular,Nanostructures,Particle Size,Protein Array Analysis,Surface Properties,Ultraviolet Rays,Water,Journal Article,Research Support, U.S. Gov't, Non-P.H.S.},
  language     = {eng},
  month        = {08},
  number       = {33},
  pages        = {9--11164},
  publisher    = {The American Chemical Society},
  series       = {Journal of the American Chemical Society},
  title        = {Bridging across length scales : multi-scale ordering of supported lipid bilayers via lipoprotein self-assembly and surface patterning},
  url          = {http://dx.doi.org/10.1021/ja803110v},
  volume       = {130},
  year         = {2008},
}