Human immunoglobulin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy, surface acoustic wave, and surface plasmon resonance techniques

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; c...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 20(2004), 14 vom: 06. Juli, Seite 5870-8
1. Verfasser: Zhou, Cheng (VerfasserIn)
Weitere Verfasser: Friedt, Jean-Michel, Angelova, Angelina, Choi, Kang-Hoon, Laureyn, Wim, Frederix, Filip, Francis, Laurent A, Campitelli, Andrew, Engelborghs, Yves, Borghs, Gustaaf
Format: Aufsatz
Sprache:English
Veröffentlicht: 2004
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Immunoglobulin G Water 059QF0KO0R Quartz 14808-60-7 Gold 7440-57-5
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245 1 0 |a Human immunoglobulin adsorption investigated by means of quartz crystal microbalance dissipation, atomic force microscopy, surface acoustic wave, and surface plasmon resonance techniques 
264 1 |c 2004 
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500 |a Date Revised 26.10.2019 
500 |a published: Print 
500 |a Citation Status MEDLINE 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
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700 1 |a Friedt, Jean-Michel  |e verfasserin  |4 aut 
700 1 |a Angelova, Angelina  |e verfasserin  |4 aut 
700 1 |a Choi, Kang-Hoon  |e verfasserin  |4 aut 
700 1 |a Laureyn, Wim  |e verfasserin  |4 aut 
700 1 |a Frederix, Filip  |e verfasserin  |4 aut 
700 1 |a Francis, Laurent A  |e verfasserin  |4 aut 
700 1 |a Campitelli, Andrew  |e verfasserin  |4 aut 
700 1 |a Engelborghs, Yves  |e verfasserin  |4 aut 
700 1 |a Borghs, Gustaaf  |e verfasserin  |4 aut 
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