Measurements of water sorption enthalpy on polymer surfaces and its effect on protein adsorption

The molar enthalpy of sorption (ΔHms`) of water vapor onto three polymer surfaces and its effect on nonspecific protein adsorption were investigated by inverse gas chromatography (IGC). The values of ΔHms measured by IGC were found to be −16.9 ± 1.2, −18.6 ± 1.3, and −29.9 ± 2.4 kJ/mole for polystyrene (PS), polymethylmethacrylate (PMMA), and poly(2-hydroxyethyl methacrylate) (PHEMA), respectively, over a temperature range of 333–423 K. Protein adsorption to three polymer-coated substrates was conducted as a function of the bulk protein concentration using lysozyme, fibrinogen, and bovine serum albumin (BSA), and the amount of adsorbed protein was measured by the solution depletion method. For a given bulk protein concentration, a larger amount of protein is adsorbed on PS and PMMA surfaces which have greater ΔHms than that of PHEMA surfaces. Although ΔHms for PS and PMMA are close to each other, PS surfaces were found to exhibit a higher adsorption affinity than PMMA surfaces over the proteins and concentrations investigated. Our results indicate that the strength of water–polymer interactions and the functional groups on the polymer surface are important factors for controlling the amount of nonspecifically adsorbed protein.