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Protein adsorption properties of OEG monolayers and dense PNIPAM brushes probed by neutron reflectivity

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Abstract

The structure of dense poly(N-isopropylacrylamide) (PNIPAM) brushes and oligo(ethylene glycol) (OEG) monolayers has been probed using neutron reflectometry and ellipsometry. The PNIPAM brush is swollen below the Lower Critical Solution Temperature (LCST) of 32 C and is collapsed at 37 C. Neutron reflectivity shows that below the LCST, the brush is described by a two-layer model: an inner dense layer and a hydrated outer layer. Above the LCST the collapsed brush forms a homogenous layer. With a fully deuterated myoglobin protein to increase the neutron scattering length density contrast, the reflectivity data show no detectable primary adsorption on the grafted OEG surface. A bound on the ternary adsorption onto PNIPAM chains forming dense brushes below and above the LCST is obtained.

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Correspondence to M. Sferrazza.

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Brouette, N., Xue, C., Haertlein, M. et al. Protein adsorption properties of OEG monolayers and dense PNIPAM brushes probed by neutron reflectivity. Eur. Phys. J. Spec. Top. 213, 343–353 (2012). https://doi.org/10.1140/epjst/e2012-01681-4

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