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Quantitative interpretation of gold nanoparticle-based bioassays designed for detection of immunocomplex formation

Zhou, Ye; Xu, Hongxing LU ; Dahlin, Andreas LU ; Vallkil, Jacob LU ; Borrebaeck, Carl LU ; Wingren, Christer LU ; Liedberg, Bo and Höök, Fredrik LU (2007) In Biointerphases 2(1). p.6-15
Abstract
The authors present in this paper how the extended Mie theory can be used to translate not only end-point data but also temporal variations of extinction peak-position changes, peak(t), into absolute mass uptake, (t), upon biomacromolecule binding to localized surface plasmon resonance (SPR) active nanoparticles (NPs). The theoretical analysis is applied on a novel sensor template composed of a three-layer surface architecture based on (i) a self-assembled monolayer of HS(CH2)15COOH, (ii) a 1:1 mixture of biotinylated and pure poly(L-lysine)-graft-poly(ethylene glycol) (PLL-g-PEG), and (iii) NeutrAvidin. Assisted by independent estimations of the thickness of the three-layer architecture using quartz crystal microbalance with dissipation... (More)
The authors present in this paper how the extended Mie theory can be used to translate not only end-point data but also temporal variations of extinction peak-position changes, peak(t), into absolute mass uptake, (t), upon biomacromolecule binding to localized surface plasmon resonance (SPR) active nanoparticles (NPs). The theoretical analysis is applied on a novel sensor template composed of a three-layer surface architecture based on (i) a self-assembled monolayer of HS(CH2)15COOH, (ii) a 1:1 mixture of biotinylated and pure poly(L-lysine)-graft-poly(ethylene glycol) (PLL-g-PEG), and (iii) NeutrAvidin. Assisted by independent estimations of the thickness of the three-layer architecture using quartz crystal microbalance with dissipation (QCM-D) monitoring, excellent agreement with parallel mass-uptake estimations using planar SPR is obtained. Furthermore, unspecific binding of serum to PLL-g-PEG was shown to be below the detection limit, making the surface architecture ideally suited for label-free detection of immunoreactions. To ensure that the immunocomplex formation occurred within the limited sensing depth (~10 nm) of the NPs, a compact model system composed of a biotinylated human recombinant single-chain antibody fragment (~2 nm) directed against cholera toxin was selected. By tracking changes in the centroid (center of mass) of the extinction peak, rather than the actual peak position, signal-to-noise levels and long-term stability upon cholera toxin detection are demonstrated to be competitive with results obtained using conventional SPR and state-of-the-art QCM-D data. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biointerphases
volume
2
issue
1
pages
6 - 15
publisher
AVS
external identifiers
  • wos:000256466800002
  • scopus:33846820443
ISSN
1934-8630
DOI
10.1116/1.2700235
language
English
LU publication?
yes
id
7518cb89-c976-4b6c-83e4-c3de71f7005e (old id 809677)
date added to LUP
2008-01-07 11:50:42
date last changed
2017-01-01 07:37:44
@article{7518cb89-c976-4b6c-83e4-c3de71f7005e,
  abstract     = {The authors present in this paper how the extended Mie theory can be used to translate not only end-point data but also temporal variations of extinction peak-position changes, peak(t), into absolute mass uptake, (t), upon biomacromolecule binding to localized surface plasmon resonance (SPR) active nanoparticles (NPs). The theoretical analysis is applied on a novel sensor template composed of a three-layer surface architecture based on (i) a self-assembled monolayer of HS(CH2)15COOH, (ii) a 1:1 mixture of biotinylated and pure poly(L-lysine)-graft-poly(ethylene glycol) (PLL-g-PEG), and (iii) NeutrAvidin. Assisted by independent estimations of the thickness of the three-layer architecture using quartz crystal microbalance with dissipation (QCM-D) monitoring, excellent agreement with parallel mass-uptake estimations using planar SPR is obtained. Furthermore, unspecific binding of serum to PLL-g-PEG was shown to be below the detection limit, making the surface architecture ideally suited for label-free detection of immunoreactions. To ensure that the immunocomplex formation occurred within the limited sensing depth (~10 nm) of the NPs, a compact model system composed of a biotinylated human recombinant single-chain antibody fragment (~2 nm) directed against cholera toxin was selected. By tracking changes in the centroid (center of mass) of the extinction peak, rather than the actual peak position, signal-to-noise levels and long-term stability upon cholera toxin detection are demonstrated to be competitive with results obtained using conventional SPR and state-of-the-art QCM-D data.},
  author       = {Zhou, Ye and Xu, Hongxing and Dahlin, Andreas and Vallkil, Jacob and Borrebaeck, Carl and Wingren, Christer and Liedberg, Bo and Höök, Fredrik},
  issn         = {1934-8630},
  language     = {eng},
  number       = {1},
  pages        = {6--15},
  publisher    = {AVS},
  series       = {Biointerphases},
  title        = {Quantitative interpretation of gold nanoparticle-based bioassays designed for detection of immunocomplex formation},
  url          = {http://dx.doi.org/10.1116/1.2700235},
  volume       = {2},
  year         = {2007},
}