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- Taussig, Michael J., et al.
(författare)
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ProteomeBinders : planning a European resource of affinity reagents for analysis of the human proteome
- 2007
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Ingår i: Nature Methods. - : Springer Science and Business Media LLC. - 1548-7091 .- 1548-7105. ; 4:1, s. 13-17
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Tidskriftsartikel (refereegranskat)abstract
- ProteomeBinders is a new European consortium aiming to establish a comprehensive resource of well-characterized affinity reagents, including but not limited to antibodies, for analysis of the human proteome. Given the huge diversity of the proteome, the scale of the project is potentially immense but nevertheless feasible in the context of a pan-European or even worldwide coordination.
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| 2. |
- Zhou, Ye, et al.
(författare)
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Quantitative interpretation of gold nanoparticle-based bioassays designed for detection of immunocomplex formation
- 2007
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Ingår i: BIOINTERPHASES. - : American Vacuum Society. - 1559-4106 .- 1934-8630. ; 2:1
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Tidskriftsartikel (refereegranskat)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, 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.
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| 10. |
- Borrebaeck, Carl, et al.
(författare)
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High-throughput proteomics using antibody microarrays: an update
- 2007
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Ingår i: Expert Review of Molecular Diagnostics. - : Informa UK Limited. - 1744-8352 .- 1473-7159. ; 7:5, s. 673-686
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Forskningsöversikt (refereegranskat)abstract
- Antibody-based microarrays are a rapidly emerging technology that has advanced from the first proof-of-concept studies to demanding serum protein profiling applications during recent years, displaying great promise within disease proteomics. Miniaturized micro- and nanoarrays can be fabricated with an almost infinite number of antibodies carrying the desired specificities. While consuming only minute amounts of reagents, multiplexed and ultrasensitive assays can be performed targeting high- as well as low-abundance analytes in complex nonfractionated proteomes. The microarray images generated can then be converted into protein expression profiles or protein atlases, revealing a detailed composition of the sample. The technology will provide unique opportunities for fields such as disease diagnostics, biomarker discovery, patient stratification, predicting disease recurrence and drug target discovery. This review describes an update of high-throughput proteomics, using antibody-based microarrays, focusing on key technological advances and novel applications that have emerged over the last 3 years.
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