- Open Access
Characterization of protein resistant, grafted methacrylate polymer layers bearing oligo(ethylene glycol) and phosphorylcholine side chains by neutron reflectometry
© American Vacuum Society 2007
Received: 19 December 2006
Accepted: 31 January 2007
Neutron reflectometry was used to investigate the structures of end-tethered protein resistant polymer layers based on poly(oligo(ethylene glycol) methyl ether methacrylate) [poly(OEGMA)] and poly(2-methacryloyloxyethyl phosphorylcholine) [poly(MPC)]. Layers having different graft densities were studied in both the dry and wet states. A stretched parabolic model was used to fit the neutron data, resulting in a one-dimensional scattering length density profile of the polymer volume fraction normal to the film. Measured in D2O, the cutoff thicknesses of OEGMA and MPC layers at high graft density (0.39 chains/nm2 for OEGMA and 0.30 chains/nm2 for MPC) and a chain length of 200 repeat units were 450 and 470 Å, respectively, close to their contour length of 500 Å, suggesting that the grafts become highly hydrated when exposed to water. It was also found that at similar graft density and chain length, the volume fraction profiles of poly(OEGMA) and poly(MPC) layers are similar, in line with the authors’ previous results showing that these surfaces have similar protein resistance [W. Feng et al., BioInterphases 1, 50 (2006)]. The possible correlation of protein resistance to water content as indicated by the average number of water molecules per ethylene oxide (N w,EO ) or phosphorylcholine (N w,PC ) moiety was investigated. N w,EO and N w,PC , estimated from the volume fraction data, increased with decreasing graft density, and when compared to the reported number of water molecules in the hydration layers of EO and PC residues, led to the conclusion that water content slightly greater than the water of hydration resulted in protein resistant surfaces, whereas water content either less than or greatly in excess of the water of hydration resulted in layers of reduced protein resistance.