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|Title: ||Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding|
|Authors: ||Le Brun, AP|
|Keywords: ||Membrane Proteins|
|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.|
|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. © 2011, MDPI Publishing|
|Appears in Collections:||Journal Articles|
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