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Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding

Lookup NU author(s): Anton Le Brun, Dr Deepan Shah, Professor Jeremy Lakey

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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.


Publication metadata

Author(s): Le Brun AP, Shah DSH, Athey D, Holt SA, Lakey JH

Publication type: Article

Publication status: Published

Journal: International Journal of Molecular Sciences

Year: 2011

Volume: 12

Issue: 8

Pages: 5157-5167

Print publication date: 15/08/2011

ISSN (electronic): 1422-0067

Publisher: MDPI AG

URL: http://dx.doi.org/10.3390/ijms1208515710

DOI: 10.3390/ijms12085157


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