ArticleElectrophoresis2013
Modeling of protein electrophoresis in silica colloidal crystals having brush layers of polyacrylamide.
Article in Electrophoresis, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Comparison of separation modes for microchip electrophoresis of proteins.Journal of separation science · 2021Article
- Electrophoresis of megaDalton proteins inside colloidal silica.Electrophoresis · 2019Article
- Nanofluidic crystals: nanofluidics in a close-packed nanoparticle array.Lab on a chip · 2017Review
- Submicrometer particles and slip flow in liquid chromatography.Analytical chemistry · 2015Article
- Silica colloidal crystals as emerging materials for high-throughput protein electrophoresis.The AAPS journal · 2013Article
- Polyacrylamide brush layer for hydrophilic interaction liquid chromatography of intact glycoproteins.Journal of chromatography. A · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Sieving of proteins in silica colloidal crystals of millimeter dimensions is characterized for particle diameters of nominally 350 and 500 nm, where the colloidal crystals are chemically modified with a brush layer of polyacrylamide. A model is developed that relates the reduced electrophoretic mobility to the experimentally measurable porosity. The model fits the data with no adjustable parameters for the case of silica colloidal crystals packed in capillaries, for which independent measurements of the pore radii were made from flow data. The model also fits the data for electrophoresis in a highly ordered colloidal crystal formed in a channel, where the unknown pore radius was used as a fitting parameter. Plate heights as small as 0.4 μm point to the potential for miniaturized separations. Band broadening increases as the pore radius approaches the protein radius, indicating that the main contribution to broadening is the spatial heterogeneity of the pore radius. The results quantitatively support the notion that sieving occurs for proteins in silica colloidal crystals, and facilitate design of new separations that would benefit from miniaturization.
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Registered trials
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