Ef. Murphy et al., Characterization of protein adsorption at the phosphorylcholine incorporated polymer-water interface, MACROMOLEC, 33(12), 2000, pp. 4545-4554
We have studied the adsorption of a number of model proteins onto the surfa
ce of a crosslinkable hydrogel polymer incorporated with phosphorylcholine
(PC) groups and dodecyl chains (PC 100B). The structure of the coated thin
polymer film was determined by neutron reflection combined with spectroscop
ic ellipsometry. No measurable change in the thickness of the polymer film
was detected within the experimental time scale of minutes when immersed in
water, showing a fast water solubilization process. The polymer film at th
e solid-water interface was modeled using a single layer of 51 +/- 3 Angstr
om with 40 +/- 5% water, suggesting a uniform distribution of water across
the polymer film. This film structure is in sharp contrast with the uneven
swelling of the film formed from a different hydrogel polymer (PC 100A) whi
ch had a similar molar ratio of dodecyl. chains and PC groups but did not c
ontain any silyl groups as cross-linkers. The results hence suggest that th
e uniform structure of the PC 100B film is rendered by the formation of the
silyl cross-linking network. The effectiveness of the PC 100B film at redu
cing protein adsorption under different solution conditions was subsequentl
y characterized. Both neutron reflection and spectroscopic ellipsometry sho
wed substantial reduction in protein adsorption on PC 100B. At the bulk pro
tein concentration around 1 g dm(-3) the surface excess was found to be les
s than 1 mg m(-2) for lysozyme and fibrinogen at pH 7 and BSA at pH 5, whil
e under the same solution conditions, the surface excess at. the hydrophili
c silicon oxide-water interface was 3.6 +/- 0.3 mg m(-2) for lysozyme, 6.0
+/- 0.3 mg m(-2) for fibrinogen, and 2.5 +/- 0.3 mg m(-2) for BSA. Despite
the structural difference between the two coated polymer films, the residua
l level of protein adsorption was found to be comparable between the two PC
polymer surfaces. The insensitivity of spectroscopic ellipsometry to the p
resence of a diffuse protein layer on the surface of the coated polymer fil
ms is also discussed.