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dc.contributor.authorLe Brun, AP-
dc.contributor.authorShah, DSH-
dc.contributor.authorAthey, D-
dc.contributor.authorHolt, SA-
dc.contributor.authorLakey, JH-
dc.identifier.citationLe 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/ijms12085157en_AU
dc.description.abstractBacterial 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 Publishingen_AU
dc.publisherMDPI Publishingen_AU
dc.subjectMembrane Proteinsen_AU
dc.titleSelf-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Bindingen_AU
dc.typeJournal Articleen_AU
Appears in Collections:Journal Articles

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