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Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of membrane proteins

Jamshad, Mohammed ; Grimard, Vinciane ; Idini, Ilaria LU ; Knowles, Tim J. ; Dowle, Miriam R. ; Schofield, Naomi ; Sridhar, Pooja ; Lin, Yupin ; Finka, Rachael and Wheatley, Mark , et al. (2015) In Nano Research 8(3). p.774-789
Abstract

In the past few years there has been a growth in the use of nanoparticles for stabilizing lipid membranes that contain embedded proteins. These bionanoparticles provide a solution to the challenging problem of membrane protein isolation by maintaining a lipid bilayer essential to protein integrity and activity. We have previously described the use of an amphipathic polymer (poly(styrene-co-maleic acid), SMA) to produce discoidal nanoparticles with a lipid bilayer core containing the embedded protein. However the structure of the nanoparticle itself has not yet been determined. This leaves a major gap in understanding how the SMA stabilizes the encapsulated bilayer and how the bilayer relates physically and structurally to an... (More)

In the past few years there has been a growth in the use of nanoparticles for stabilizing lipid membranes that contain embedded proteins. These bionanoparticles provide a solution to the challenging problem of membrane protein isolation by maintaining a lipid bilayer essential to protein integrity and activity. We have previously described the use of an amphipathic polymer (poly(styrene-co-maleic acid), SMA) to produce discoidal nanoparticles with a lipid bilayer core containing the embedded protein. However the structure of the nanoparticle itself has not yet been determined. This leaves a major gap in understanding how the SMA stabilizes the encapsulated bilayer and how the bilayer relates physically and structurally to an unencapsulated lipid bilayer. In this paper we address this issue by describing the structure of the SMA lipid particle (SMALP) using data from small angle neutron scattering (SANS), electron microscopy (EM), attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), differential scanning calorimetry (DSC) and nuclear magnetic resonance spectroscopy (NMR). We show that the particle is disc shaped containing a polymer “bracelet” encircling the lipid bilayer. The structure and orientation of the individual components within the bilayer and polymer are determined showing that styrene moieties within SMA intercalate between the lipid acyl chains. The dimensions of the encapsulated bilayer are also determined and match those measured for a natural membrane. Taken together, the description of the structure of the SMALP forms the foundation for future development and applications of SMALPs in membrane protein production and analysis.

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publishing date
type
Contribution to journal
publication status
published
keywords
detergent, lipid, membrane proteins, nanoparticles, polymer, structure
in
Nano Research
volume
8
issue
3
pages
16 pages
publisher
Springer
external identifiers
  • scopus:84925465471
ISSN
1998-0124
DOI
10.1007/s12274-014-0560-6
language
English
LU publication?
no
additional info
Publisher Copyright: © 2015, Tsinghua University Press and Springer-Verlag Berlin Heidelberg.
id
44ab9f1e-64ca-4e4e-9919-498608023b6b
date added to LUP
2023-03-29 11:49:49
date last changed
2023-03-31 14:05:40
@article{44ab9f1e-64ca-4e4e-9919-498608023b6b,
  abstract     = {{<p>In the past few years there has been a growth in the use of nanoparticles for stabilizing lipid membranes that contain embedded proteins. These bionanoparticles provide a solution to the challenging problem of membrane protein isolation by maintaining a lipid bilayer essential to protein integrity and activity. We have previously described the use of an amphipathic polymer (poly(styrene-co-maleic acid), SMA) to produce discoidal nanoparticles with a lipid bilayer core containing the embedded protein. However the structure of the nanoparticle itself has not yet been determined. This leaves a major gap in understanding how the SMA stabilizes the encapsulated bilayer and how the bilayer relates physically and structurally to an unencapsulated lipid bilayer. In this paper we address this issue by describing the structure of the SMA lipid particle (SMALP) using data from small angle neutron scattering (SANS), electron microscopy (EM), attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), differential scanning calorimetry (DSC) and nuclear magnetic resonance spectroscopy (NMR). We show that the particle is disc shaped containing a polymer “bracelet” encircling the lipid bilayer. The structure and orientation of the individual components within the bilayer and polymer are determined showing that styrene moieties within SMA intercalate between the lipid acyl chains. The dimensions of the encapsulated bilayer are also determined and match those measured for a natural membrane. Taken together, the description of the structure of the SMALP forms the foundation for future development and applications of SMALPs in membrane protein production and analysis.</p><p>[Figure not available: see fulltext.]</p>}},
  author       = {{Jamshad, Mohammed and Grimard, Vinciane and Idini, Ilaria and Knowles, Tim J. and Dowle, Miriam R. and Schofield, Naomi and Sridhar, Pooja and Lin, Yupin and Finka, Rachael and Wheatley, Mark and Thomas, Owen R.T. and Palmer, Richard E. and Overduin, Michael and Govaerts, Cédric and Ruysschaert, Jean-Marie and Edler, Karen J. and Dafforn, Tim R.}},
  issn         = {{1998-0124}},
  keywords     = {{detergent; lipid; membrane proteins; nanoparticles; polymer; structure}},
  language     = {{eng}},
  number       = {{3}},
  pages        = {{774--789}},
  publisher    = {{Springer}},
  series       = {{Nano Research}},
  title        = {{Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of membrane proteins}},
  url          = {{http://dx.doi.org/10.1007/s12274-014-0560-6}},
  doi          = {{10.1007/s12274-014-0560-6}},
  volume       = {{8}},
  year         = {{2015}},
}