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The adsorption of chicken egg white lysozyme at the functionalized silicon oxide−solution interface has been studied using the combined measurement of spectroscopic ellipsometry and neutron reflection. The solid oxide surface was modified by coating a self-assembled monolayer of pentadecyltrichlorosilane with terminal hydroxyl groups (abbreviated to C 15 OH). Neutron reflection measurement at the solid−D 2 O interface showed that the C 15 OH layer was 16 ± 2 Å thick and the volume fraction was 0.94 ± 0.05, suggesting the formation of a close-packed monolayer. The adsorption of lysozyme was made at pH 4 and 7 with lysozyme concentration ranging from 0.03 to 4 g dm - 3 . The results were then compared with those from previous studies at the hydrophilic SiO 2 −water and the hydrophobed SiO 2 −water interfaces, with the latter formed by coating a monolayer of octadecyl trichlorosilane (abbreviated to OTS). At 0.03 g dm - 3 and pH 7 the surface excess was found to be 0.6 ± 0.3 mg m - 2 at the C 15 OH−water interface, as compared with 1.7 mg m - 2 at the SiO 2 −water interface and 1.9 mg m - 2 at the OTS−water interface. As lysozyme concentration is increased to 4 g dm - 3, the surface excess at the C 15 OH−water interface reaches 2.1 mg m - 2, as compared with 4.7 mg m - 2 at the hydrophilic SiO 2 −water interface and 5.1 mg m - 2 at the OTS−water interface. These values demonstrate the attainment of the minimum surface excess on the hydroxyl surface. Shifting solution pH from 7 to 4 reduces adsorption on all the surfaces studied, but the lowest level of adsorption is again obtained on the hydroxyl surface. The reversibility of the adsorption at the C 15 OH−water interface was examined by cycling the solution pH at different lysozyme concentrations. Adsorption was found to be completely reversible at the low lysozyme concentration of 1 g dm - 3, while at the high concentration of 4 g dm - 3 the adsorption was irreversible.
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Su et al. (2000) studied this question.
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