Improving Mouse Monoclonal Antibody Binding to Protein Arrays
Author Information
Author(s): Le Brun Anton P., Shah Deepan S. H., Athey Dale, Holt Stephen A., Lakey Jeremy H.
Primary Institution: Institute for Cell and Molecular Biosciences, The Medical School, Newcastle University
Hypothesis
Can a novel protein design reduce the dissociation of mouse monoclonal IgG from a protein array?
Conclusion
The introduction of a flexible linker between Z domains increases the capacity for IgG binding, enhancing the signal and sensitivity of the array.
Supporting Evidence
- The engineered protein showed improved binding of mouse monoclonal IgG compared to previous designs.
- Surface plasmon resonance confirmed the successful assembly of the protein on gold.
- The flexible linker allowed for better interaction with antibodies, increasing binding capacity.
Takeaway
Scientists created a new protein that helps mouse antibodies stick better to a surface, making tests more reliable.
Methodology
The study involved engineering a scaffold protein with Z domains linked by a flexible polypeptide linker and testing its binding properties using surface plasmon resonance.
Digital Object Identifier (DOI)
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