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

Author： Le Brun Anton P.   Shah Deepan S. H.   Athey Dale   Holt Stephen A.   Lakey Jeremy H.  

Publisher： MDPI

E-ISSN： 1422-0067|12|8|5157-5167

ISSN： 1422-0067

Source： International Journal of Molecular Sciences, Vol.12, Iss.8, 2011-08, pp. : 5157-5167

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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.

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