Self-assembly of protein monolayers engineered for improved monoclonal immunoglobulin G binding
dc.contributor.author | Le Brun, AP | en_AU |
dc.contributor.author | Shah, DSH | en_AU |
dc.contributor.author | Athey, D | en_AU |
dc.contributor.author | Holt, SA | en_AU |
dc.contributor.author | Lakey, JH | en_AU |
dc.date.accessioned | 2011-12-14T00:42:06Z | en_AU |
dc.date.available | 2011-12-14T00:42:06Z | en_AU |
dc.date.issued | 2011-08-01 | en_AU |
dc.date.statistics | 2011-12-14 | en_AU |
dc.description.abstract | Bacterial outer membrane proteins, along with a filling lipid molecule can be modified to form stable self-assembled monolayers on gold. The transmembrane domain of Escherichia coli outer membrane protein A has been engineered to create a scaffold protein to which functional motifs can be fused. In earlier work we described the assembly and structure of an antibody-binding array where the Z domain of Staphylococcus aureus protein A was fused to the scaffold protein. Whilst the binding of rabbit polyclonal immunoglobulin G (IgG) to the array is very strong, mouse monoclonal IgG dissociates from the array easily. This is a problem since many immunodiagnostic tests rely upon the use of mouse monoclonal antibodies. Here we describe a strategy to develop an antibody-binding array that will bind mouse monoclonal IgG with lowered dissociation from the array. A novel protein consisting of the scaffold protein fused to two pairs of Z domains separated by a long flexible linker was manufactured. Using surface plasmon resonance the self-assembly of the new protein on gold and the improved binding of mouse monoclonal IgG were demonstrated. © The Authors - This is an open access article distributed under the Creative Commons Attribution License | en_AU |
dc.identifier.citation | Le Brun, A.P., Shah, D.S.H., Athey, D., Holt, S.A., Lakey, J.H. (2011). Self-assembly of protein monolayers engineered for improved monoclonal immunoglobulin G binding. International Journal of Molecular Sciences, 12(8), 5157-5167. doi:10.3390/ijms12085157 | en_AU |
dc.identifier.govdoc | 3871 | en_AU |
dc.identifier.issn | 1661-6596 | en_AU |
dc.identifier.issue | 8 | en_AU |
dc.identifier.journaltitle | International Journal of Molecular Sciences | en_AU |
dc.identifier.pagination | 5157-5167 | en_AU |
dc.identifier.uri | http://dx.doi.org/10.3390/ijms12085157 | en_AU |
dc.identifier.uri | http://apo.ansto.gov.au/dspace/handle/10238/3948 | en_AU |
dc.identifier.volume | 12 | en_AU |
dc.language.iso | en | en_AU |
dc.publisher | MDPI Publishing | en_AU |
dc.subject | Membrane proteins | en_AU |
dc.subject | Gold | en_AU |
dc.subject | Immunoglobulins | en_AU |
dc.subject | Resonance | en_AU |
dc.subject | Surfaces | en_AU |
dc.subject | Molecules | en_AU |
dc.title | Self-assembly of protein monolayers engineered for improved monoclonal immunoglobulin G binding | en_AU |
dc.type | Journal Article | en_AU |