Exploring the interfacial structure of protein adsorbates and the kinetics of protein adsorption: an in situ high-energy X-ray reflectivity study.
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.
Evers
Florian
F
Fakultät Physik/DELTA, Technische Universität Dortmund, Maria-Goeppert-Mayer-Strasse 2, Dortmund, Germany, florian.evers@tu-dortmund.de
Shokuie
Kaveh
K
Paulus
Michael
M
Sternemann
Christian
C
Czeslik
Claus
C
Tolan
Metin
M
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
D011506:Proteins; D012996:Solutions; D009113:Muramidase