Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/74219
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Type: Journal article
Title: Immobilized Streptavidin gradients as bioconjugation platforms
Author: Coad, B.
Vasilev, K.
Diener, K.
Hayball, J.
Short, R.
Griesser, H.
Citation: Langmuir: the ACS journal of surfaces and colloids, 2012; 28(5):2710-2717
Publisher: Amer Chemical Soc
Issue Date: 2012
ISSN: 0743-7463
1520-5827
Statement of
Responsibility: 
Bryan R. Coad, Krasimir Vasilev, Kerrilyn R. Diener, John D. Hayball, Robert D. Short and Hans J. Griesser
Abstract: Surface density gradients of streptavidin (SAV) were created on solid surfaces and demonstrated functionality as a bioconjugation platform. The surface density of immobilized streptavidin steadily increased in one dimension from 0 to 235 ng cm(-2) over a distance of 10 mm. The density of coupled protein was controlled by its immobilization onto a polymer surface bearing a gradient of aldehyde group density, onto which SAV was covalently linked using spontaneous imine bond formation between surface aldehyde functional groups and primary amine groups on the protein. As a control, human serum albumin was immobilized in the same manner. The gradient density of aldehyde groups was created using a method of simultaneous plasma copolymerization of ethanol and propionaldehyde. Control over the surface density of aldehyde groups was achieved by manipulating the flow rates of these vapors while moving a mask across substrates during plasma discharge. Immobilized SAV was able to bind biotinylated probes, indicating that the protein retained its functionality after being immobilized. This plasma polymerization technique conveniently allows virtually any substrate to be equipped with tunable protein gradients and provides a widely applicable method for bioconjugation to study effects arising from controllable surface densities of proteins.
Keywords: Humans
Biotin
Polymers
Serum Albumin
Streptavidin
Biotinylation
Surface Properties
Rights: Copyright © 2012 American Chemical Society
DOI: 10.1021/la204714p
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