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Ellipsometry studies of protein layers adsorbed at hydrophobic surfaces
YKI – Ytkemiska institutet.
1994 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 166, 333-342 p.Article in journal (Refereed)
Abstract [en]

The adsorption of some model proteins, human serum albumin (HSA), IgG, fibrinogen and lysozyme, at methylated silica surfaces was investigated with in situ ellipsometry. By performing studies with the bare substrate at two different ambient refractive indices, and by performing 4-zone averaging, the adsorbed amount, the adsorbed layer thickness and the mean adsorbed layer refractive index are obtained. The adsorbed amounts obtained for the proteins agree well with previous results. The adsorbed layer thicknesses vary strongly between the proteins. Thus, at adsorption plateau, the adsorbed layer thicknesses (del) obtained for HSA, lysozyme, IgG and fibrinogen are 4±2 nm, 11±2 nm, 18±2 nm and 28±2 nm, respectively. The build-up of the adsorbed layers proceeds differently for different proteins. Thus, for fibrinogen, both del and the adsorbed layer mean refractive index (nf) increase monotonically up to about 4 mg/m2. For IgG, on the other hand, del is essentially independent of the adsorbed amount, whereas nf increases linearly. Finally, the adsorbed layer formed by lysozyme is more compact than those formed by fibrinogen, IgG and HSA. These findings are discussed in terms of adsorbed layer structure.

Place, publisher, year, edition, pages
1994. Vol. 166, 333-342 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26768OAI: oai:DiVA.org:ri-26768DiVA: diva2:1053771
Note
A925Available from: 2016-12-08 Created: 2016-12-08Bibliographically approved

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