Human Immunoglobulin Adsorption Investigated by Means of Quartz Crystal Microbalance Dissipation, Atomic Force Microscopy, Surface Acoustic Wave, and Surface Plasmon Resonance Techniques
| Autor: | Andrew Campitelli, Jean-Michel Friedt, Cheng Zhou, Filip Frederix, Wim Laureyn, Yves Engelborghs, Gustaaf Borghs, Laurent Francis, Kang-Hoon Choi, Angelina Angelova |
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| Rok vydání: | 2004 |
| Předmět: |
Time Factors
Materials science Surface Properties Analytical chemistry Microscopy Atomic Force Sensitivity and Specificity law.invention Adsorption law Microscopy Monolayer Electrochemistry Humans General Materials Science Surface plasmon resonance Crystallization Spectroscopy Surface acoustic wave Water Quartz Surfaces and Interfaces Quartz crystal microbalance Surface Plasmon Resonance Condensed Matter Physics Kinetics Immunoglobulin G Gold Hydrophobic and Hydrophilic Interactions |
| Zdroj: | Langmuir. 20:5870-5878 |
| ISSN: | 1520-5827 0743-7463 |
| DOI: | 10.1021/la036251d |
| Popis: | 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/SAW measurements. 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. |
| Databáze: | OpenAIRE |
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