Antibody adsorption and orientation on hydrophobic surfaces

The orientation of a monoclonal, anti-streptavidin human IgG1 antibody on a model hydrophobic, CH(3)-terminated surface (1-dodecanethiol self-assembled monolayer on gold) was studied by monitoring the mechanical coupling between the adsorbed layer and the surface as well as the binding of molecular...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 28(2012), 3 vom: 24. Jan., Seite 1765-74
1. Verfasser: Wiseman, Meredith E (VerfasserIn)
Weitere Verfasser: Frank, Curtis W
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2012
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Antibodies, Monoclonal Bacterial Proteins Immunoglobulin Fab Fragments Immunoglobulin G Receptors, Fc Sulfhydryl Compounds dodecylmercaptan mehr... 112-55-0 Serum Albumin, Bovine 27432CM55Q Gold 7440-57-5 Streptavidin 9013-20-1
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520 |a The orientation of a monoclonal, anti-streptavidin human IgG1 antibody on a model hydrophobic, CH(3)-terminated surface (1-dodecanethiol self-assembled monolayer on gold) was studied by monitoring the mechanical coupling between the adsorbed layer and the surface as well as the binding of molecular probes to the antibodies. In this study, the streptavidin antigen was used as a probe for the Fab portions of the antibody, while bacteria-derived Protein G' was used as a probe for the Fc region. Bovine serum albumin (BSA) acted as a blocking protein. Monolayer coverage occurred around 468 ng/cm(2). Below 100 ng/cm(2), antibodies were found to adsorb flat-on, tightly coupled to the surface and unable to capture their antigen, whereas the Fc region was able to bind Protein G'. At half-monolayer coverage, there was a transition in the mechanism of adsorption to allow for vertically oriented antibodies, as evidenced by the binding of both Protein G' and streptavidin as well as looser mechanical coupling with the surface. Monolayer coverage was characterized by a reduced level in probe binding per antibody and an even less rigid coupling to the surface 
650 4 |a Journal Article 
650 4 |a Research Support, N.I.H., Extramural 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Antibodies, Monoclonal  |2 NLM 
650 7 |a Bacterial Proteins  |2 NLM 
650 7 |a Immunoglobulin Fab Fragments  |2 NLM 
650 7 |a Immunoglobulin G  |2 NLM 
650 7 |a Receptors, Fc  |2 NLM 
650 7 |a Sulfhydryl Compounds  |2 NLM 
650 7 |a dodecylmercaptan  |2 NLM 
650 7 |a 112-55-0  |2 NLM 
650 7 |a Serum Albumin, Bovine  |2 NLM 
650 7 |a 27432CM55Q  |2 NLM 
650 7 |a Gold  |2 NLM 
650 7 |a 7440-57-5  |2 NLM 
650 7 |a Streptavidin  |2 NLM 
650 7 |a 9013-20-1  |2 NLM 
700 1 |a Frank, Curtis W  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Langmuir : the ACS journal of surfaces and colloids  |d 1992  |g 28(2012), 3 vom: 24. Jan., Seite 1765-74  |w (DE-627)NLM098181009  |x 1520-5827  |7 nnns 
773 1 8 |g volume:28  |g year:2012  |g number:3  |g day:24  |g month:01  |g pages:1765-74 
856 4 0 |u http://dx.doi.org/10.1021/la203095p  |3 Volltext 
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