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https://apo.ansto.gov.au/dspace/handle/10238/3948
Title: | Self-assembly of protein monolayers engineered for improved monoclonal immunoglobulin G binding |
Authors: | Le Brun, AP Shah, DSH Athey, D Holt, SA Lakey, JH |
Keywords: | Membrane proteins Gold Immunoglobulins Resonance Surfaces Molecules |
Issue Date: | 1-Aug-2011 |
Publisher: | MDPI Publishing |
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 |
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 |
Gov't Doc #: | 3871 |
URI: | http://dx.doi.org/10.3390/ijms12085157 http://apo.ansto.gov.au/dspace/handle/10238/3948 |
ISSN: | 1661-6596 |
Appears in Collections: | Journal Articles |
Files in This Item:
File | Description | Size | Format | |
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ijms-12-05157-v2.pdf | 466.86 kB | Adobe PDF | ![]() View/Open |
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