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Chemical Grafting of Poly(ethylene glycol) Methyl Ether Methacrylate ontoPolymer Surfaces by Atmospheric Pressure Plasma Processing

Biomedical Sciences Research Institute Computer Science Research Institute Environmental Sciences Research Institute Nanotechnology & Advanced Materials Research Institute

D'Sa, R and Meenan, BJ (2010) Chemical Grafting of Poly(ethylene glycol) Methyl Ether Methacrylate ontoPolymer Surfaces by Atmospheric Pressure Plasma Processing. Langmuir, 26 (3). pp. 1894-1903. [Journal article]

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URL: http://pubs.acs.org/doi/abs/10.1021/la902654y

DOI: 10.1021/la902654y


This article reports the use of atmospheric pressure plasma processing to induce chemical grafting of poly(ethylene glycol) methyl ether methacrylate (PEGMA) onto polystyrene (PS) and poly(methyl methacrylate) (PMMA) surfaces with the aim of attaining an adlayer conformation which is resistant to protein adsorption. The plasma treatment was carried out using a dielectric barrier discharge (DBD) reactor with PEGMA of molecular weights (MW) 1000 and 2000, PEGMA1000 and PEGMA2000, being grafted in a two step procedure: (1) reactive groups are generated on the polymer surface followed by (2) radical addition reactions with the PEGMA. The surface chemistry, coherency, and topography of the resulting PEGMA grafted surfaces were characterized by X-ray photoelectron spectroscopy (XPS), time-of-flight secondary ion mass spectrometry (ToF-SIMS), and atomic force microscopy (AFM), respectively. The most coherently grafted PEGMA layers were observed for the 2000 MW PEGMA macromolecule, DBD processed at an energy dose of 105.0 J/cm2 as indicated by ToF-SIMS images. The effect of the chemisorbed PEGMA layer on protein adsorption was assessed by evaluating the surface response to bovine serum albumin (BSA) using XPS. BSA was used as a model protein to determine the grafted macromolecular conformation of the PEGMA layer. Whereas the PEGMA1000 surfaces showed some protein adsorption, the PEGMA2000 surfaces appeared to absorb no measurable amount of protein, confirming the optimum surface conformation for a nonfouling surface.

Item Type:Journal article
Faculties and Schools:Faculty of Computing & Engineering
Faculty of Computing & Engineering > School of Engineering
Research Institutes and Groups:Engineering Research Institute
Engineering Research Institute > Nanotechnology & Integrated BioEngineering Centre (NIBEC)
ID Code:12534
Deposited By:Professor Brian Meenan
Deposited On:25 Mar 2010 15:25
Last Modified:18 Aug 2011 11:16

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