Bridging across length scales : multi-scale ordering of supported lipid bilayers via lipoprotein self-assembly and surface patterning
(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
- 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
- publishing date
- 2008-08-20
- 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 (ACS)
- external identifiers
-
- pmid:18642906
- 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
- 2024-01-14 08:07:09
@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}},
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.}},
language = {{eng}},
month = {{08}},
number = {{33}},
pages = {{9--11164}},
publisher = {{The American Chemical Society (ACS)}},
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}},
doi = {{10.1021/ja803110v}},
volume = {{130}},
year = {{2008}},
}