Characterization of protein adsorption at the phosphorylcholine incorporated polymer-water interface

Citation
Ef. Murphy et al., Characterization of protein adsorption at the phosphorylcholine incorporated polymer-water interface, MACROMOLEC, 33(12), 2000, pp. 4545-4554
Citations number
35
Categorie Soggetti
Organic Chemistry/Polymer Science
Journal title
MACROMOLECULES
ISSN journal
00249297 → ACNP
Volume
33
Issue
12
Year of publication
2000
Pages
4545 - 4554
Database
ISI
SICI code
0024-9297(20000613)33:12<4545:COPAAT>2.0.ZU;2-0
Abstract
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.