Characterizing the structure of protein layers adsorbed onto functionalized surfaces by means of in-situ X-ray reflectivity

In a biological cell, proteins face a highly complex environment comprising crowding and confinement effects as well as interactions with interfaces, cosolvents, and other biomolecules. In this study, the X-ray reflectivity technique has been used for the in-situ characterization of adsorbed protein...

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Bibliographic Details
Published in:The European physical journal. ST, Special topics Special topics, 2009-02, Vol.167 (1), p.185-189
Main Authors: Evers, F., Shokuie, K., Paulus, M., Tiemeyer, S., Sternemann, Ch, Czeslik, C., Tolan, M.
Format: Article
Language:English
Subjects:
Atomic
Classical and Continuum Physics
Condensed Matter Physics
Condensed matter: structure, mechanical and thermal properties
Exact sciences and technology
Materials Science
Measurement Science and Instrumentation
Molecular
Optical and Plasma Physics
Physics
Physics and Astronomy
Regular Article
Solid surfaces and solid-solid interfaces
Solid-fluid interfaces
Surfaces and interfaces
thin films and whiskers (structure and nonelectronic properties)
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Summary:In a biological cell, proteins face a highly complex environment comprising crowding and confinement effects as well as interactions with interfaces, cosolvents, and other biomolecules. In this study, the X-ray reflectivity technique has been used for the in-situ characterization of adsorbed protein layers at solid-liquid interfaces. The adsorption of bovine serum albumin at the hydrophobic polystyrene-water interface has been investigated in the presence and in the absence of salts. The data indicate that enhanced adsorption occurs at high salt concentrations.
ISSN:1951-6355
1951-6401
DOI:10.1140/epjst/e2009-00956-1