Please use this identifier to cite or link to this item:
|Title:||Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding|
|Authors:||Le Brun, AP|
|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. © 2011, MDPI Publishing|
|Gov't Doc #:||3871|
|Appears in Collections:||Journal Articles|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.