Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/72613
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Type: Journal article
Title: Functionality of Proteins Bound to Plasma Polymer Surfaces
Author: Coad, B.
Scholz, T.
Vasilev, K.
Hayball, J.
Short, R.
Griesser, H.
Citation: ACS Applied Materials and Interfaces, 2012; 4(5):2455-2463
Publisher: American Chemical Society
Issue Date: 2012
ISSN: 1944-8244
1944-8252
Statement of
Responsibility: 
Bryan R. Coad, Tanja Scholz, Krasimir Vasilev, John D. Hayball, Robert D. Short and Hans J. Griesser
Abstract: The deposition of a thin film layer by plasma polymerization enables the surface functionalization of a wide range of substrate materials for biointerfacial interactions. Plasma polymers can surface-bind proteins specifically via covalent linkages or nonspecifically through other irreversible adsorption mechanisms; key questions are whether covalent chemisorption has indeed occurred, and whether the protein retains functionality. Here the mode of surface binding of streptavidin and the biotin binding functionality of the bound streptavidin layer are studied on plasma polymer (pp) surfaces deposited using propionaldehyde and ethanol that were plasma polymerized at different powers (P) to investigate possible mechanisms for protein binding to a range of different surface chemistries. As expected, with pp surfaces composed principally of aldehyde groups, protein conjugation appears to be specific (chemisorption) allowing the immobilization of streptavidin (SAV) molecules retaining the ability to bind biotinylated probes. To contrast with this, we present the first study of protein adsorption to ethanol pp surfaces prepared at different P. This provides an investigation into retention of the hydroxyl functionality in the pp at low P and its effect on protein adsorption. Adsorption of human serum albumin (HSA) to ethanol pp was similar to that on propionaldehyde pp except at low P (5 W) where hydroxyl group retention and hydration presumably has a role in reducing protein adsorption. Although we observed SAV adsorption to ethanol pp surfaces at all P, interestingly, the protein lost its ability to bind biotinylated probes. Thus we suggest that irreversible, nonspecific adsorption of protein on ethanol pp surfaces results in apparent protein denaturation despite the hydrophilic nature of the ethanol pp surface. We conclude by making inferences between the pp structure as measured by X-ray photoelectron spectroscopy (XPS) and the related protein adsorption mechanisms.
Keywords: biomaterial interface engineering; plasma polymerization; bioconjugation; ethanol plasma polymer; propionaldehyde plasma polymer; aldehyde surface; biointerfaces; biomaterial surfaces; protein adsorption
Rights: Copyright © 2012 American Chemical Society
RMID: 0020119305
DOI: 10.1021/am300128n
Appears in Collections:Medicine publications

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