Human immunoglobulin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy, surface acoustic wave, and surface plasmon resonance techniques |
| |
Authors: | Zhou Cheng Friedt Jean-Michel Angelova Angelina Choi Kang-Hoon Laureyn Wim Frederix Filip Francis Laurent A Campitelli Andrew Engelborghs Yves Borghs Gustaaf |
| |
Institution: | Biosensors group, Interuniversity Microelectronics Center (IMEC), Kapeldreef 75, 3001 Leuven, Belgium. Cheng.zhou@imec.be |
| |
Abstract: | 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|