Next Article in Journal
Major Histocompatibility Complex (MHC) Markers in Conservation Biology
Next Article in Special Issue
Syntheses and Self-assembling Behaviors of Pentagonal Conjugates of Tryptophane Zipper-Forming Peptide
Previous Article in Journal
Enhancing Single Molecule Imaging in Optofluidics and Microfluidics
Previous Article in Special Issue
Enhanced Chiral Recognition by Cyclodextrin Dimers
Article

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

1
Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University, Framlington Place, Newcastle upon Tyne, NE2 4HH, UK
2
Orla Protein Technologies Ltd, Biosciences Centre, International Centre for Life, Times Square, Newcastle upon Tyne, NE1 4EP, UK
3
ISIS Neutron Facility, STFC Rutherford Appleton Laboratory, Harwell Science and Innovation Campus, Didcot, Oxfordshire, OX11 0QX, UK
*
Author to whom correspondence should be addressed.
Current address: Bragg Institute, Australian Nuclear Science and Technology Organisation, Locked Bag 2001, Kirrawee DC, NSW 2232, Australia.
Int. J. Mol. Sci. 2011, 12(8), 5157-5167; https://doi.org/10.3390/ijms12085157
Received: 4 July 2011 / Revised: 4 July 2011 / Accepted: 10 August 2011 / Published: 15 August 2011
(This article belongs to the Special Issue Molecular Self-Assembly 2011)
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. View Full-Text
Keywords: membrane protein; gold; immunoglobulin; self-assembled monolayer; surface plasmon resonance membrane protein; gold; immunoglobulin; self-assembled monolayer; surface plasmon resonance
Show Figures

MDPI and ACS Style

Le Brun, A.P.; Shah, D.S.H.; Athey, D.; Holt, S.A.; Lakey, J.H. Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding. Int. J. Mol. Sci. 2011, 12, 5157-5167. https://doi.org/10.3390/ijms12085157

AMA Style

Le Brun AP, Shah DSH, Athey D, Holt SA, Lakey JH. Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding. International Journal of Molecular Sciences. 2011; 12(8):5157-5167. https://doi.org/10.3390/ijms12085157

Chicago/Turabian Style

Le Brun, Anton P., Deepan S. H. Shah, Dale Athey, Stephen A. Holt, and Jeremy H. Lakey 2011. "Self-Assembly of Protein Monolayers Engineered for Improved Monoclonal Immunoglobulin G Binding" International Journal of Molecular Sciences 12, no. 8: 5157-5167. https://doi.org/10.3390/ijms12085157

Find Other Styles

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Back to TopTop