liu.seSearch for publications in DiVA
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Quantitative interpretation of gold nanoparticle-based bioassays designed for detection of immunocomplex formation
Lund Univ, Div Solid State Phys, SE-22100 Lund, Sweden.
Lund Univ, Div Solid State Phys, SE-22100 Lund, Sweden.
Lund Univ, Div Solid State Phys, SE-22100 Lund, Sweden.
Lund Univ, Dept Immunotechnol, SE-22007 Lund, Sweden.
Show others and affiliations
2007 (English)In: BIOINTERPHASES, ISSN 1559-4106, Vol. 2, no 1Article in journal (Refereed) Published
Abstract [en]

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, Delta lambda(peak)(t), into absolute mass uptake, Gamma(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)(15)COOH, (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 (similar to 10 nm) of the NPs, a compact model system composed of a biotinylated human recombinant single-chain antibody fragment (empty set similar to 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. (C) 2007 American Vacuum Society.

Place, publisher, year, edition, pages
2007. Vol. 2, no 1
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-45886DOI: 10.1116/1.2700235OAI: oai:DiVA.org:liu-45886DiVA: diva2:266782
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2011-01-11

Open Access in DiVA

No full text

Other links

Publisher's full text

Authority records BETA

Liedberg, Bo

Search in DiVA

By author/editor
Liedberg, Bo
By organisation
The Institute of TechnologySensor Science and Molecular Physics
Engineering and Technology

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 86 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf