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Human Immunoglobulin Adsorption Investigated by Means of Quartz Crystal Microbalance Dissipation, Atomic Force Microscopy, Surface Acoustic Wave, and Surface Plasmon Resonance Techniques

Year: 2004

Journal: Langmuir 2004, 20, 5870-5878, 20100827

Authors: Zhou C., Friedt J-M., Angelova A., Choi K-H, Laureyn W., Frederix F., Francis L.A., Campitelli A., Engelborghs Y., Borghs G.

Last authors: Gustaaf Borghs

Organizations: Biosensors group, Interuniversity Microelectronics Center (IMEC), Kapeldreef 75, 3001 Leuven, Belgium, Laboratory of Biomolecular Dynamic, Department of Chemistry KULeuven, Celestijnenlaan 200D, 3001 Leuven, Belgium, PCPM, Université catholique de Louvain, Croix du Sud 1, 1348 Louvain-la-Neuve, Belgium

Country: Belgium

Time-resolved adsorption behavior of a human immunoglobin G (hIgG) protein on a hydrophobized gold surface is investigated using multitechniques: quartz crystal microbalance/dissipation (QCM-D) technique; combined surface plasmon resonance (SPR) and Love mode surface acoustic wave (SAW) technique; combined QCM-D and atomic force microscopy (AFM) technique. The adsorbed hIgG forms interfacial structures varying in organization from a submonolayer to a multilayer. An “end-on” IgG orientation in the monolayer film, associated with the surface coverage results, does not corroborate with the effective protein thickness determined from SPR/SAWmeasurements. This inconsistence is interpreted by a deformation effect induced by conformation change. This conformation change is confirmed by QCM-D measurement. Combined SPR/SAW measurements suggest that the adsorbed protein barely contains water after extended contact with the hydrophobic surface. This limited interfacial hydration also contributed to a continuous conformation change in the adsorbed protein layer. The viscoelastic variation associated with interfacial conformation changes induces about 1.5 times overestimation of the mass uptake in the QCM-D measurements. The merit of combined multitechnique measurements is demonstrated.