title: Exploring the interfacial structure of protein adsorbates and the kinetics of protein adsorption: an in situ high-energy X-ray reflectivity study.
abstract: The high energy X-ray reflectivity technique has been applied to study the interfacial structure of protein adsorbates and protein adsorption kinetics in situ. For this purpose, the adsorption of lysozyme at the hydrophilic silica-water interface has been chosen as a model system. The structure of adsorbed lysozyme layers was probed for various aqueous solution conditions. The effect of solution pH and lysozyme concentration on the interfacial structure was measured. Monolayer formation was observed for all cases except for the highest concentration. The adsorbed protein layers consist of adsorbed lysozyme molecules with side-on or end-on orientation. By means of time-dependent X-ray reflectivity scans, the time-evolution of adsorbed proteins was monitored as well. The results of this study demonstrate the capabilities of in situ X-ray reflectivity experiments on protein adsorbates. The great advantages of this method are the broad wave vector range available and the high time resolution.
authors: Fakultät Physik/DELTA, Technische Universität Dortmund, Maria-Goeppert-Mayer-Strasse 2, Dortmund, Germany, florian.evers@tu-dortmund.de
authors: Florian
authors: F
authors: Evers
authors: Kaveh
authors: K
authors: Shokuie
authors: Michael
authors: M
authors: Paulus
authors: Christian
authors: C
authors: Sternemann
authors: Claus
authors: C
authors: Czeslik
authors: Metin
authors: M
authors: Tolan
mesh_terms: D000327:Adsorption; D000818:Animals; D004583:Electrons; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D015233:Models, Statistical; D009113:Muramidase / Q000737:chemistry*; D017785:Photons; D011506:Proteins / Q000737:chemistry*; D015203:Reproducibility of Results; D012996:Solutions; D013499:Surface Properties; D013997:Time Factors; D014965:X-Rays
chemical_list: D011506:Proteins; D012996:Solutions; D009113:Muramidase